From dca9dafa893c3ae07ffc0e3cd2a9e6d14a86c535 Mon Sep 17 00:00:00 2001 From: "marcin p. joachimiak" <4625870+realmarcin@users.noreply.github.com> Date: Thu, 3 Sep 2026 21:24:11 -0700 Subject: [PATCH 1/3] Score causal graph readiness and enhance records --- README.md | 2 +- .../appendage/bacterial_type_flagellum.yaml | 12 + data/structures/appendage/type_iv_pilus.yaml | 86 +++++++ .../cytoskeleton/mreb_filament.yaml | 86 +++++++ .../division_machinery/divisome_complex.yaml | 23 ++ ...ton_transporting_atp_synthase_complex.yaml | 16 ++ .../envelope/cell_outer_membrane.yaml | 178 +++++++++++++++ ...ram_negative_bacterium_type_cell_wall.yaml | 187 ++++++++++++++++ .../peptidoglycan_based_cell_wall.yaml | 123 ++++++++++ data/structures/envelope/s_layer.yaml | 54 +++++ data/structures/inclusion/gas_vesicle.yaml | 204 +++++++++++++++++ .../membrane_organelle/magnetosome.yaml | 6 + .../microcompartment/carboxysome.yaml | 20 ++ .../encapsulin_nanocompartment.yaml | 198 +++++++++++++++++ data/structures/nucleoid/nucleoid.yaml | 95 ++++++++ ..._accepting_chemotaxis_protein_complex.yaml | 126 ++++++++++- .../ribonucleoprotein/ribosome.yaml | 10 + ..._iii_protein_secretion_system_complex.yaml | 102 +++++++++ ...pore_external_encapsulating_structure.yaml | 182 +++++++++++++++ .../2026-09-04T014136Z-codex-b18360.yaml | 22 ++ .../2026-09-04T014136Z-codex-d52ed9.yaml | 22 ++ .../2026-09-04T011019Z-codex-32cc8a.yaml | 25 +++ .../2026-09-04T040500Z-codex-f9c170.yaml | 21 ++ .../2026-09-04T013928Z-codex-034eb4.yaml | 23 ++ .../2026-09-04T011805Z-codex-da906f.yaml | 25 +++ .../2026-09-04T042400Z-codex-0b3903.yaml | 21 ++ .../2026-09-04T012301Z-codex-eb0cc5.yaml | 23 ++ .../2026-09-04T034957Z-codex-d32d61.yaml | 26 +++ .../2026-09-04T011557Z-codex-73a905.yaml | 26 +++ .../2026-09-04T041400Z-codex-c2ee88.yaml | 21 ++ .../2026-09-04T011223Z-codex-b5961f.yaml | 25 +++ .../2026-09-04T044300Z-codex-f64c03.yaml | 21 ++ .../2026-09-04T014136Z-codex-ea15e8.yaml | 22 ++ .../2026-09-04T043400Z-codex-99020e.yaml | 23 ++ .../2026-09-04T010327Z-codex-4abcd4.yaml | 27 +++ .../2026-09-04T011949Z-codex-9db5d8.yaml | 26 +++ .../2026-09-04T011330Z-codex-0fcf20.yaml | 26 +++ .../2026-09-04T034706Z-codex-fc9767.yaml | 27 +++ .../2026-09-04T014136Z-codex-90001a.yaml | 23 ++ .../2026-09-04T014136Z-codex-3472a5.yaml | 22 ++ .../2026-09-04T013816Z-codex-b5801a.yaml | 23 ++ .../2026-09-04T012106Z-codex-02296d.yaml | 24 ++ .../2026-09-04T005809Z-codex-a42bf8.yaml | 26 +++ justfile | 4 + .../appendage/bacterial_type_flagellum.html | 2 +- pages/structures/appendage/type_iv_pilus.html | 11 +- .../cytoskeleton/mreb_filament.html | 11 +- .../division_machinery/divisome_complex.html | 3 +- ...ton_transporting_atp_synthase_complex.html | 2 +- .../envelope/cell_outer_membrane.html | 20 +- ...ram_negative_bacterium_type_cell_wall.html | 20 +- .../peptidoglycan_based_cell_wall.html | 12 +- pages/structures/envelope/s_layer.html | 8 +- pages/structures/inclusion/gas_vesicle.html | 20 +- .../membrane_organelle/magnetosome.html | 2 +- .../microcompartment/carboxysome.html | 2 +- .../encapsulin_nanocompartment.html | 21 +- pages/structures/nucleoid/nucleoid.html | 14 +- ..._accepting_chemotaxis_protein_complex.html | 14 +- .../ribonucleoprotein/ribosome.html | 2 +- ..._iii_protein_secretion_system_complex.html | 12 +- ...pore_external_encapsulating_structure.html | 20 +- scripts/score_causal_graphs.py | 210 ++++++++++++++++++ tests/test_score_causal_graphs.py | 123 ++++++++++ tests/test_scripts.py | 8 + 65 files changed, 2798 insertions(+), 23 deletions(-) create mode 100644 history/records/bacterial_type_flagellum/2026-09-04T014136Z-codex-b18360.yaml create mode 100644 history/records/carboxysome/2026-09-04T014136Z-codex-d52ed9.yaml create mode 100644 history/records/cell_outer_membrane/2026-09-04T011019Z-codex-32cc8a.yaml create mode 100644 history/records/cell_outer_membrane/2026-09-04T040500Z-codex-f9c170.yaml create mode 100644 history/records/divisome_complex/2026-09-04T013928Z-codex-034eb4.yaml create mode 100644 history/records/encapsulin_nanocompartment/2026-09-04T011805Z-codex-da906f.yaml create mode 100644 history/records/encapsulin_nanocompartment/2026-09-04T042400Z-codex-0b3903.yaml create mode 100644 history/records/endospore_external_encapsulating_structure/2026-09-04T012301Z-codex-eb0cc5.yaml create mode 100644 history/records/endospore_external_encapsulating_structure/2026-09-04T034957Z-codex-d32d61.yaml create mode 100644 history/records/gas_vesicle/2026-09-04T011557Z-codex-73a905.yaml create mode 100644 history/records/gas_vesicle/2026-09-04T041400Z-codex-c2ee88.yaml create mode 100644 history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T011223Z-codex-b5961f.yaml create mode 100644 history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T044300Z-codex-f64c03.yaml create mode 100644 history/records/magnetosome/2026-09-04T014136Z-codex-ea15e8.yaml create mode 100644 history/records/methyl_accepting_chemotaxis_protein_complex/2026-09-04T043400Z-codex-99020e.yaml create mode 100644 history/records/mreb_filament/2026-09-04T010327Z-codex-4abcd4.yaml create mode 100644 history/records/nucleoid/2026-09-04T011949Z-codex-9db5d8.yaml create mode 100644 history/records/peptidoglycan_based_cell_wall/2026-09-04T011330Z-codex-0fcf20.yaml create mode 100644 history/records/peptidoglycan_based_cell_wall/2026-09-04T034706Z-codex-fc9767.yaml create mode 100644 history/records/proton_transporting_atp_synthase_complex/2026-09-04T014136Z-codex-90001a.yaml create mode 100644 history/records/ribosome/2026-09-04T014136Z-codex-3472a5.yaml create mode 100644 history/records/s_layer/2026-09-04T013816Z-codex-b5801a.yaml create mode 100644 history/records/type_iii_protein_secretion_system_complex/2026-09-04T012106Z-codex-02296d.yaml create mode 100644 history/records/type_iv_pilus/2026-09-04T005809Z-codex-a42bf8.yaml create mode 100644 scripts/score_causal_graphs.py create mode 100644 tests/test_score_causal_graphs.py diff --git a/README.md b/README.md index 8121b31..3a15e07 100644 --- a/README.md +++ b/README.md @@ -68,7 +68,7 @@ records, not records; phenotypes are TraitMech records. See | SECRETION_SYSTEM | 1 | | | | | SPORE | 1 | | | | -17 records are grounded in GO; 2 carry minted identifiers. 19 list components, 9 carry causal graphs (56 evidence-backed edges), 8 link to TraitMech traits, and 5 carry licensed, cited imaging evidence. +17 records are grounded in GO; 2 carry minted identifiers. 19 list components, 19 carry causal graphs (152 evidence-backed edges), 8 link to TraitMech traits, and 5 carry licensed, cited imaging evidence. Run `just report` for the live report. Every current record is diff --git a/data/structures/appendage/bacterial_type_flagellum.yaml b/data/structures/appendage/bacterial_type_flagellum.yaml index a0b2772..cd84170 100644 --- a/data/structures/appendage/bacterial_type_flagellum.yaml +++ b/data/structures/appendage/bacterial_type_flagellum.yaml @@ -558,12 +558,16 @@ causal_graphs: - subject: c_ring predicate: drives object: rotation + description: Torque on FliG and the C ring turns the MS ring, rod, hook, and filament + as a rigid flagellar rotor. evidence: - reference: DOI:10.1016/j.tim.2014.12.011 notes: The C ring, MS ring and rod rotate as one rigid rotor. - subject: rotation predicate: propels object: filament + description: Rotation is transmitted from the basal body through the hook to the + external helical filament. evidence: - reference: DOI:10.1146/annurev.biochem.72.121801.161737 notes: Rotation of the helical filament produces thrust. @@ -571,6 +575,8 @@ causal_graphs: predicate: enables object: swimming predicate_id: RO:0002327 + description: The rotating helical filament acts as a propeller that generates + thrust for swimming motility. evidence: - reference: DOI:10.1146/annurev.biochem.72.121801.161737 notes: Berg 2003. @@ -698,5 +704,11 @@ curation_history: reviewed UniProt examples, type=family entries, and unchanged family consensus across curated scope examples. llm_assisted: true +- timestamp: '2026-09-04T01:40:08Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Added descriptions to the remaining flagellar torque-generation edges so + every edge now states the mechanistic step it represents. + llm_assisted: true xrefs: - uniprot.location:SL-0307 diff --git a/data/structures/appendage/type_iv_pilus.yaml b/data/structures/appendage/type_iv_pilus.yaml index 120a4f7..e865c73 100644 --- a/data/structures/appendage/type_iv_pilus.yaml +++ b/data/structures/appendage/type_iv_pilus.yaml @@ -71,6 +71,85 @@ functions: evidence: - reference: DOI:10.1038/nrmicro.2017.40 notes: A comprehensive guide to pilus biogenesis in Gram-negative bacteria. +causal_graphs: +- graph_id: extension_retraction_twitching + title: PilB and PilT drive type IV pilus extension-retraction cycles + description: The extension ATPase assembles pilin subunits into the extracellular + filament, and the retraction ATPase pulls an attached filament back through the + envelope. Surface-attached retraction generates the force used for twitching motility. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: extension_atpase + label: PilB-family extension ATPase + node_type: GENE_OR_PROTEIN + component_ref: extension_atpase + - node_id: major_pilin + label: major type IV pilin + node_type: GENE_OR_PROTEIN + component_ref: major_pilin + - node_id: pilus_filament + label: type IV pilus filament + node_type: STRUCTURE + grounding: GO:0044096 + - node_id: surface_bound_pilus + label: surface-bound type IV pilus + node_type: STATE + - node_id: retraction_atpase + label: PilT-family retraction ATPase + node_type: GENE_OR_PROTEIN + component_ref: retraction_atpase + - node_id: twitching_motility + label: type IV pilus-dependent motility + node_type: BIOLOGICAL_PROCESS + grounding: GO:0043107 + edges: + - subject: extension_atpase + predicate: extends + object: pilus_filament + description: The cytoplasmic PilB-family ATPase powers pilus extension from the + inner-membrane assembly platform. + evidence: + - reference: DOI:10.1038/nrmicro.2017.40 + notes: Hospenthal, Costa and Waksman 2017 review the PilB-family ATPase as the + motor that extends Gram-negative type IV pili. + - subject: major_pilin + predicate: polymerizes into + object: pilus_filament + description: Major pilin subunits form the surface-exposed type IV pilus polymer. + evidence: + - reference: DOI:10.1038/nrmicro.2017.40 + notes: Hospenthal, Costa and Waksman 2017 describe T4P fibres as polymers of + pilin subunits assembled by the biogenesis machinery. + - subject: pilus_filament + predicate: reaches + object: surface_bound_pilus + description: Extension projects the pilus outward so its distal end can bind a + surface or neighboring cell. + evidence: + - reference: DOI:10.1073/pnas.121171698 + notes: Skerker and Berg 2001 directly observed Pseudomonas aeruginosa type IV + pili extending, attaching at their distal ends and retracting. + - subject: retraction_atpase + predicate: retracts + object: surface_bound_pilus + description: The PilT-family ATPase depolymerizes the attached filament back into + the envelope. + evidence: + - reference: DOI:10.1038/35024105 + notes: Merz, So and Sheetz 2000 measured Neisseria gonorrhoeae pilus retraction + and showed that force generation and motility require PilT. + - subject: surface_bound_pilus + predicate: pulls cell during + object: twitching_motility + description: Retraction of a surface-bound filament pulls the cell body forward. + evidence: + - reference: DOI:10.1038/35024105 + notes: Merz, So and Sheetz 2000 used laser tweezers to show that T4P filaments + retract with enough force to move cells. + - reference: DOI:10.1073/pnas.121171698 + notes: Skerker and Berg 2001 directly observed Pseudomonas aeruginosa pili alternating + extension and retraction during surface motility. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-30T19:30:00Z' @@ -107,6 +186,13 @@ curation_history: and exact GO identity, preserved annotation quality metadata, and stored no imaging volumes. llm_assisted: true +- timestamp: '2026-09-04T00:58:09Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a DOI-backed FUNCTION graph for the PilB/PilT extension-retraction + cycle that assembles type IV pili and pulls surface-bound cells during twitching + motility. + llm_assisted: true datasets: - accession: CryoETDataPortal:10155 title: Bdellovibrio attack-phase diff --git a/data/structures/cytoskeleton/mreb_filament.yaml b/data/structures/cytoskeleton/mreb_filament.yaml index 8411adc..e723163 100644 --- a/data/structures/cytoskeleton/mreb_filament.yaml +++ b/data/structures/cytoskeleton/mreb_filament.yaml @@ -84,6 +84,84 @@ evidence: - reference: DOI:10.1016/j.cell.2018.02.050 notes: 'Shi H, Bratton BP, Gitai Z, Huang KC 2018, ''How to Build a Bacterial Cell: MreB as the Foreman of E. coli Construction'', Cell.' +causal_graphs: +- graph_id: filament_guided_sidewall_synthesis + title: MreB and RodZ orient sidewall synthesis to preserve a rod + description: MreB subunits form membrane-associated filaments that RodZ couples + to the elongasome. Those filaments orient circumferential sidewall peptidoglycan + synthesis, and the resulting feedback keeps rod-shaped cells from widening into + spheres. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: mreb + label: MreB + node_type: GENE_OR_PROTEIN + component_ref: mreb + - node_id: mreb_filament + label: MreB filament + node_type: STRUCTURE + grounding: cellstructuremech:mreb_filament + - node_id: rodz + label: RodZ + node_type: GENE_OR_PROTEIN + component_ref: elongasome_link + - node_id: elongasome + label: elongasome + node_type: STRUCTURE + grounding: cellstructuremech:elongasome + - node_id: sidewall_synthesis + label: sidewall peptidoglycan biosynthetic process + node_type: BIOLOGICAL_PROCESS + grounding: GO:0009252 + - node_id: rod_shape + label: rod shaped + node_type: TRAIT + grounding: METPO:1000681 + edges: + - subject: mreb + predicate: polymerizes into + object: mreb_filament + description: MreB monomers assemble into short membrane-bound filaments. + evidence: + - reference: DOI:10.1016/j.cell.2018.02.050 + notes: Shi, Bratton, Gitai and Huang 2018 review E. coli MreB filament architecture + and membrane association. + - subject: rodz + predicate: couples + object: elongasome + description: RodZ bridges MreB filaments to the cell-wall synthesis machinery. + evidence: + - reference: DOI:10.1016/j.cell.2018.02.050 + notes: Shi, Bratton, Gitai and Huang 2018 review cytoplasmic RodZ-MreB binding + and periplasmic RodZ contacts with wall-synthesis enzymes. + - subject: mreb_filament + predicate: orients + object: elongasome + description: Curvature-biased filaments constrain where and in which direction + the Rod complex inserts new wall. + evidence: + - reference: DOI:10.1016/j.cell.2018.02.050 + notes: Shi, Bratton, Gitai and Huang 2018 describe MreB as a curvature sensor + that both detects and changes local shape. + - subject: elongasome + predicate: carries out + object: sidewall_synthesis + description: The elongasome is the RodA/PBP2 peptidoglycan synthase complex that + builds the cylindrical sidewall. + evidence: + - reference: DOI:10.1038/nrmicro2677 + notes: Typas, Banzhaf, Gross and Vollmer 2011 review the elongation complex + that builds sidewall peptidoglycan. + - subject: sidewall_synthesis + predicate: maintains + object: rod_shape + description: Circumferential sidewall insertion elongates the cylinder and maintains + rod-like shape. + evidence: + - reference: DOI:10.1016/j.cell.2018.02.050 + notes: Shi, Bratton, Gitai and Huang 2018 describe MreB-driven cell-wall feedback + as the self-organizing system for rod shape maintenance. discussions: - discussion_id: first_minted_identifier prompt: This is the corpus's first minted identifier — is the scheme right? @@ -168,6 +246,14 @@ curation_history: cell-shape claim it was attached to. The paper remains cited elsewhere on this record, and the three verbatim snippets are unaffected.' llm_assisted: true +- timestamp: '2026-09-04T00:58:09Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph for MreB/RodZ-guided sidewall synthesis that points + at the separate elongasome record, cites the existing MreB shape review and the + elongasome's sidewall-synthesis review, and keeps the filament-to-machine relation + out of equivalence-only xrefs. + llm_assisted: true associated_traits: - trait_id: METPO:1000681 trait_label: rod shaped diff --git a/data/structures/division_machinery/divisome_complex.yaml b/data/structures/division_machinery/divisome_complex.yaml index f0ad52d..65a7207 100644 --- a/data/structures/division_machinery/divisome_complex.yaml +++ b/data/structures/division_machinery/divisome_complex.yaml @@ -123,6 +123,9 @@ causal_graphs: - node_id: ring label: FtsZ ring node_type: STRUCTURE + - node_id: treadmilling + label: FtsZ treadmilling + node_type: BIOLOGICAL_PROCESS - node_id: synthase label: FtsW-FtsI septal synthase node_type: GENE_OR_PROTEIN @@ -135,15 +138,27 @@ causal_graphs: - subject: tether predicate: anchors object: ftsz + description: FtsA, ZipA or SepF-family membrane tethers attach FtsZ protofilaments + to the cytoplasmic membrane at the division site. evidence: - reference: DOI:10.1146/annurev-biophys-121219-081703 notes: 'McQuillen & Xiao 2020: FtsA and ZipA hold FtsZ filaments at the membrane.' - subject: ftsz predicate: assembles into object: ring + description: Membrane-tethered FtsZ filaments polymerize into the cytokinetic + Z ring at midcell. evidence: - reference: DOI:10.1146/annurev-biophys-121219-081703 notes: McQuillen & Xiao 2020 describe filament assembly into the Z ring at midcell. + - subject: ftsz + predicate: treadmills within + object: ring + description: Dynamic FtsZ filaments treadmill around the circumference of the + ring. + evidence: + - reference: DOI:10.1146/annurev-biophys-121219-081703 + notes: McQuillen & Xiao 2020 review FtsZ treadmilling around the division site. - subject: ring predicate: distributes object: synthase @@ -156,6 +171,8 @@ causal_graphs: - subject: synthase predicate: carries out object: septum + description: FtsW-FtsI enzymes synthesize the septal peptidoglycan that closes + the division plane. evidence: - reference: DOI:10.1146/annurev-biophys-121219-081703 notes: 'McQuillen & Xiao 2020: FtsW-FtsI builds the septal peptidoglycan.' @@ -214,6 +231,12 @@ curation_history: vitro EM studies ( 93 , 183 )'' -- inventing reference numbers a reader could have chased. `just evidence-verify` refused all four before they could be committed.' llm_assisted: true +- timestamp: '2026-09-04T01:38:58Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Added an explicit FtsZ treadmilling node and descriptions to the divisome + graph so its septal-synthase distribution mechanism is fully represented. + llm_assisted: true - timestamp: '2026-09-03T00:10:07Z' curator: claude action: CORRECT_UNIT diff --git a/data/structures/energy_complex/proton_transporting_atp_synthase_complex.yaml b/data/structures/energy_complex/proton_transporting_atp_synthase_complex.yaml index d7d3b59..9df38aa 100644 --- a/data/structures/energy_complex/proton_transporting_atp_synthase_complex.yaml +++ b/data/structures/energy_complex/proton_transporting_atp_synthase_complex.yaml @@ -173,6 +173,8 @@ causal_graphs: - subject: pmf predicate: drives ion flow through object: a + description: The proton motive force drives ions through offset half-channels + in subunit a at the a/c-ring interface. evidence: - reference: DOI:10.1146/annurev-biochem-013118-110903 notes: 'Kuehlbrandt 2019: ions cross via the two offset half-channels in subunit @@ -189,12 +191,16 @@ causal_graphs: - subject: cring predicate: rotates object: stalk + description: Ion-driven rotation of the membrane c-ring carries the attached central + stalk as one rotor. evidence: - reference: DOI:10.1146/annurev-biochem-013118-110903 notes: 'Kuehlbrandt 2019: the c-ring and central stalk rotate as one rotor.' - subject: stalk predicate: drives conformational cycling of object: head + description: The asymmetric rotating central stalk forces catalytic beta subunits + in the alpha3beta3 head through sequential conformations. evidence: - reference: DOI:10.1146/annurev-biochem-013118-110903 notes: Kuehlbrandt 2019 describes the asymmetric gamma subunit imposing the @@ -203,6 +209,8 @@ causal_graphs: predicate: catalyses formation of object: atp predicate_id: RO:0002327 + description: Catalytic nucleotide-binding interfaces in the F1 head synthesize + ATP from ADP and phosphate. evidence: - reference: DOI:10.1146/annurev-biochem-013118-110903 notes: 'Kuehlbrandt 2019: ATP is synthesised at the catalytic interfaces of @@ -210,6 +218,8 @@ causal_graphs: - subject: head predicate: participates in object: synthesis + description: The F1 head is the catalytic sector of the proton-motive-force-driven + ATP synthase. evidence: - reference: DOI:10.1146/annurev-biochem-013118-110903 notes: Kuehlbrandt 2019 reviews rotary catalysis as the mechanism of ATP synthesis. @@ -250,6 +260,12 @@ curation_history: and polymer-entity links, and left alternate assembly stoichiometries unflattened at RCSB. No molecular render was ingested. llm_assisted: true +- timestamp: '2026-09-04T01:40:08Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Added descriptions to ATP synthase rotary-catalysis edges so every edge + states the ion-flow, rotor, or catalytic step it represents. + llm_assisted: true datasets: - accession: PDB:6OQR title: E. coli ATP Synthase ADP State 1a diff --git a/data/structures/envelope/cell_outer_membrane.yaml b/data/structures/envelope/cell_outer_membrane.yaml index bb7203d..a8ccee3 100644 --- a/data/structures/envelope/cell_outer_membrane.yaml +++ b/data/structures/envelope/cell_outer_membrane.yaml @@ -54,6 +54,170 @@ functions: evidence: - reference: DOI:10.1101/cshperspect.a000414 notes: The bacterial cell envelope. +causal_graphs: +- graph_id: lps_bam_outer_membrane_barrier + title: Lpt and BAM assemble the asymmetric permeability barrier + description: The Lpt transenvelope machine delivers LPS to the cell surface, while + the BAM complex folds and inserts beta-barrel proteins into the outer membrane. + LPS concentrated in the outer leaflet and OMP beta barrels together form the asymmetric + permeability barrier that distinguishes the diderm envelope. + graph_kind: ASSEMBLY + scope_status: MECHANISTIC + nodes: + - node_id: lpt_machine + label: Lpt transenvelope LPS transport machine + node_type: GENE_OR_PROTEIN + - node_id: lipopolysaccharide + label: lipopolysaccharide-rich outer leaflet + node_type: CHEMICAL + component_ref: lipopolysaccharide + grounding: CHEBI:16412 + - node_id: bam_complex + label: beta-barrel assembly machinery complex + node_type: GENE_OR_PROTEIN + - node_id: outer_membrane_beta_barrels + label: outer-membrane beta-barrel proteins + node_type: GENE_OR_PROTEIN + component_ref: outer_membrane_beta_barrels + - node_id: asymmetric_outer_membrane + label: asymmetric outer membrane + node_type: STRUCTURE + grounding: GO:0009279 + - node_id: permeability_barrier + label: selective permeability barrier + node_type: CAPACITY + edges: + - subject: lpt_machine + predicate: transports to the outer leaflet + object: lipopolysaccharide + description: LptBFGC/A/DE moves LPS from the inner membrane, across the periplasm + and through LptD/E for insertion into the outer leaflet. + evidence: + - reference: DOI:10.1074/jbc.R117.802512 + notes: Sperandeo, Martorana and Polissi 2017 review LPS transport across the + envelope and assembly at the outer-membrane outer leaflet. + - subject: lipopolysaccharide + predicate: forms + object: asymmetric_outer_membrane + description: LPS occupies the outer leaflet while phospholipids are concentrated + in the inner leaflet. + evidence: + - reference: DOI:10.1101/cshperspect.a000414 + notes: Silhavy, Kahne and Walker 2010 describe the outer membrane as a lipid + bilayer with phospholipids confined to the inner leaflet and LPS in the outer + leaflet. + - subject: bam_complex + predicate: folds and inserts + object: outer_membrane_beta_barrels + description: BAM catalyzes assembly of OMP beta barrels into the outer membrane. + evidence: + - reference: DOI:10.1146/annurev-biochem-061408-144611 + notes: Hagan, Silhavy and Kahne 2011 review beta-barrel membrane-protein assembly + by the Bam complex. + - subject: outer_membrane_beta_barrels + predicate: embed in + object: asymmetric_outer_membrane + description: OMP beta barrels are the integral transmembrane protein class of + the outer membrane. + evidence: + - reference: DOI:10.1101/cshperspect.a000414 + notes: Silhavy, Kahne and Walker 2010 describe nearly all integral transmembrane + outer-membrane proteins as beta barrels. + - subject: asymmetric_outer_membrane + predicate: enables + object: permeability_barrier + description: The LPS-rich outer leaflet excludes many toxic hydrophobic molecules, + while porin beta barrels admit selected hydrophilic solutes. + evidence: + - reference: DOI:10.1101/cshperspect.a000414 + notes: Silhavy, Kahne and Walker 2010 tie the tightly packed LPS leaflet to + the hydrophobic barrier and beta-barrel porins to selected small-molecule + diffusion. +- graph_id: lps_porin_selective_permeability + title: LPS and beta-barrel porins tune selective permeability + description: Lipopolysaccharide forms a densely packed outer leaflet that slows + hydrophobic toxin entry, while beta-barrel porins provide size- and chemistry-limited + routes for hydrophilic solutes, jointly creating the selective permeability + barrier of the outer membrane. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: lipopolysaccharide + label: lipopolysaccharide-rich outer leaflet + node_type: CHEMICAL + component_ref: lipopolysaccharide + grounding: CHEBI:16412 + - node_id: ordered_lps_layer + label: tightly packed LPS surface layer + node_type: STRUCTURE + - node_id: hydrophobic_compounds + label: hydrophobic toxic compounds + node_type: CHEMICAL + - node_id: beta_barrel_porins + label: beta-barrel porin channels + node_type: GENE_OR_PROTEIN + component_ref: outer_membrane_beta_barrels + - node_id: hydrophilic_solutes + label: hydrophilic solutes + node_type: CHEMICAL + - node_id: selective_permeability_barrier + label: selective permeability barrier + node_type: CAPACITY + edges: + - subject: lipopolysaccharide + predicate: packs into + object: ordered_lps_layer + description: LPS molecules in the outer leaflet pack into an ordered surface + layer that restricts diffusion through the lipid phase. + evidence: + - reference: DOI:10.1128/MMBR.67.4.593-656.2003 + notes: Nikaido 2003 reviews how LPS organization makes the outer membrane a + low-permeability barrier. + - subject: ordered_lps_layer + predicate: excludes + object: hydrophobic_compounds + description: The ordered LPS layer inhibits nonspecific penetration by hydrophobic + antibiotics, detergents, and other toxic molecules. + evidence: + - reference: DOI:10.1128/MMBR.67.4.593-656.2003 + notes: Nikaido 2003 explains that the outer leaflet blocks hydrophobic solutes + that would otherwise partition through ordinary phospholipid bilayers. + - subject: beta_barrel_porins + predicate: channel + object: hydrophilic_solutes + description: Porin beta barrels provide water-filled diffusion paths for small + hydrophilic solutes that cannot readily cross the LPS-rich lipid phase. + evidence: + - reference: DOI:10.1128/MMBR.67.4.593-656.2003 + notes: Nikaido 2003 reviews porin-mediated diffusion across Gram-negative + outer membranes. + - subject: beta_barrel_porins + predicate: filter + object: hydrophilic_solutes + description: Pore size and channel properties limit which hydrophilic solutes + pass through outer-membrane porins. + evidence: + - reference: DOI:10.1128/MMBR.67.4.593-656.2003 + notes: Nikaido 2003 describes porin permeability in terms of size exclusion, + channel specificity, and diffusion rate. + - subject: ordered_lps_layer + predicate: cooperates with + object: beta_barrel_porins + description: The low-permeability LPS leaflet and selective porin channels + combine to admit useful hydrophilic molecules while reducing harmful influx. + evidence: + - reference: DOI:10.1101/cshperspect.a000414 + notes: Silhavy, Kahne and Walker 2010 connect outer-leaflet LPS and beta-barrel + porins to the outer membrane's permeability-barrier function. + - subject: beta_barrel_porins + predicate: enables + object: selective_permeability_barrier + description: Selective porin conductance superimposes controlled nutrient uptake + on the LPS-based exclusion barrier. + evidence: + - reference: DOI:10.1128/MMBR.67.4.593-656.2003 + notes: Nikaido 2003 reviews how porin diffusion and outer-leaflet LPS jointly + determine Gram-negative outer-membrane permeability. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-30T19:30:00Z' @@ -74,5 +238,19 @@ curation_history: is machine-readable rather than prose. Set per component; ASSOCIATED_MACHINERY only where the protein acts on the already-assembled structure. llm_assisted: true +- timestamp: '2026-09-04T01:09:39Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added an ASSEMBLY graph for Lpt-driven LPS transport, BAM-driven beta-barrel + OMP assembly, and the resulting asymmetric outer-membrane permeability barrier, + with additional DOI evidence on Lpt and BAM. + llm_assisted: true +- timestamp: '2026-09-04T04:03:00Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph for LPS- and beta-barrel-porin-mediated selective + permeability, grounded LPS nodes with ChEBI, and added Nikaido 2003 evidence + for hydrophobic exclusion and porin diffusion. + llm_assisted: true xrefs: - uniprot.location:SL-0040 diff --git a/data/structures/envelope/gram_negative_bacterium_type_cell_wall.yaml b/data/structures/envelope/gram_negative_bacterium_type_cell_wall.yaml index c97897c..5ae23ea 100644 --- a/data/structures/envelope/gram_negative_bacterium_type_cell_wall.yaml +++ b/data/structures/envelope/gram_negative_bacterium_type_cell_wall.yaml @@ -48,6 +48,179 @@ functions: evidence: - reference: DOI:10.1101/cshperspect.a000414 notes: The bacterial cell envelope. +causal_graphs: +- graph_id: peptidoglycan_outer_membrane_tethering + title: Lipoprotein tethers connect the thin wall to the outer membrane + description: In the canonical E. coli diderm envelope, the thin peptidoglycan sacculus + sits in the periplasm and Braun-lipoprotein tethers connect that wall to the outer + membrane. This peptidoglycan-outer membrane coupling tunes the mechanical stiffness + of the Gram-negative envelope. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: thin_peptidoglycan + label: thin peptidoglycan sacculus + node_type: STRUCTURE + component_ref: thin_peptidoglycan + - node_id: outer_membrane_lipoprotein_links + label: peptidoglycan-outer-membrane lipoprotein links + node_type: GENE_OR_PROTEIN + component_ref: outer_membrane_lipoprotein_links + xrefs: + - UniProtKB:P69776 + - Pfam:PF04728 + - node_id: outer_membrane + label: cell outer membrane + node_type: STRUCTURE + grounding: GO:0009279 + - node_id: linked_diderm_envelope + label: linked Gram-negative cell envelope + node_type: STRUCTURE + - node_id: envelope_stiffness + label: cell-envelope stiffness + node_type: QUALITY + edges: + - subject: thin_peptidoglycan + predicate: lines + object: outer_membrane + description: The Gram-negative wall is the thin peptidoglycan layer located in + the periplasm, inside the outer membrane. + evidence: + - reference: DOI:10.1101/cshperspect.a000414 + notes: Silhavy, Kahne and Walker 2010 describe the Gram-negative envelope as + an outer membrane around a thin peptidoglycan cell wall. + - subject: outer_membrane_lipoprotein_links + predicate: anchors into + object: outer_membrane + description: Lpp is anchored in the outer membrane through its N-terminal lipid. + evidence: + - reference: DOI:10.1038/s41467-020-15489-1 + notes: Mathelié-Guinlet and colleagues 2020 describe Lpp as inserted in the + E. coli outer membrane by a lipid moiety on its N-terminal cysteine. + - subject: outer_membrane_lipoprotein_links + predicate: covalently tethers + object: thin_peptidoglycan + description: A subset of Lpp molecules covalently connect the outer membrane to + diaminopimelic-acid residues in peptidoglycan. + evidence: + - reference: DOI:10.1038/s41467-020-15489-1 + notes: Mathelié-Guinlet and colleagues 2020 studied E. coli Lpp mutations that + alter the covalent peptidoglycan linkage. + - subject: outer_membrane_lipoprotein_links + predicate: connects + object: linked_diderm_envelope + description: Lpp-like tethers physically connect the outer membrane and the thin + wall into one mechanically coupled envelope. + evidence: + - reference: DOI:10.1038/s41467-020-15489-1 + notes: Mathelié-Guinlet and colleagues 2020 show that Lpp contributes to envelope + stiffness by covalently connecting the outer membrane to peptidoglycan. + - subject: linked_diderm_envelope + predicate: controls + object: envelope_stiffness + description: The peptidoglycan layer, the outer membrane and the proteins that + connect them together determine diderm cell-envelope mechanics. + evidence: + - reference: DOI:10.1038/s41467-020-15489-1 + notes: Mathelié-Guinlet and colleagues 2020 measured E. coli envelope mechanics + after genetically changing Lpp length and its peptidoglycan attachment site. +- graph_id: lpp_lol_pg_tether_assembly + title: Lol trafficking and L,D-transpeptidation install Lpp wall tethers + description: Braun lipoprotein matures as a triacylated outer-membrane lipoprotein, + is trafficked to the outer membrane by the Lol pathway, and is covalently attached + to meso-diaminopimelate in peptidoglycan by L,D-transpeptidases. The result is + a protein bridge from the outer membrane to the thin Gram-negative wall. + graph_kind: ASSEMBLY + scope_status: MECHANISTIC + nodes: + - node_id: lpp + label: Braun lipoprotein Lpp + node_type: GENE_OR_PROTEIN + component_ref: outer_membrane_lipoprotein_links + xrefs: + - UniProtKB:P69776 + - Pfam:PF04728 + - node_id: mature_lpp + label: triacylated mature Lpp + node_type: GENE_OR_PROTEIN + xrefs: + - UniProtKB:P69776 + - Pfam:PF04728 + - node_id: lol_pathway + label: Lol lipoprotein-trafficking pathway + node_type: GENE_OR_PROTEIN + - node_id: outer_membrane + label: cell outer membrane + node_type: STRUCTURE + grounding: GO:0009279 + - node_id: ldt_lpp + label: Lpp-anchoring L,D-transpeptidases + node_type: GENE_OR_PROTEIN + - node_id: thin_peptidoglycan + label: thin peptidoglycan sacculus + node_type: STRUCTURE + component_ref: thin_peptidoglycan + - node_id: lpp_pg_tether + label: covalent Lpp-peptidoglycan tether + node_type: STRUCTURE + edges: + - subject: lpp + predicate: matures into + object: mature_lpp + description: Lpp enters the bacterial lipoprotein maturation pathway and becomes + a triacylated lipoprotein with an N-terminal lipidated cysteine. + evidence: + - reference: DOI:10.1098/rstb.2015.0030 + notes: Konovalova and Silhavy 2015 review outer-membrane lipoprotein maturation + and trafficking through the Lol pathway. + - subject: lol_pathway + predicate: traffics + object: mature_lpp + description: LolCDE, LolA, and LolB move mature outer-membrane lipoproteins from + the inner membrane through the periplasm to the outer membrane. + evidence: + - reference: DOI:10.1073/pnas.1702248114 + notes: Grabowicz and Silhavy 2017 summarize the Lol trafficking paradigm and + test which Lol components remain essential when lipoprotein accumulation at + the inner membrane is prevented. + - subject: mature_lpp + predicate: inserts into + object: outer_membrane + description: The mature Lpp N-terminal lipid anchors the lipoprotein in the + outer membrane. + evidence: + - reference: DOI:10.1038/s41467-020-15489-1 + notes: Mathelie-Guinlet and colleagues 2020 describe E. coli Lpp as embedded + in the outer membrane through its N-terminal lipid moiety. + - subject: ldt_lpp + predicate: attaches + object: mature_lpp + description: The L,D-transpeptidases ErfK, YcfS, and YbiS can link the C-terminal + lysine of Lpp to peptidoglycan stem peptides. + evidence: + - reference: DOI:10.1128/JB.00084-07 + notes: Magnet et al. 2007 identified ErfK, YcfS, and YbiS as E. coli + L,D-transpeptidases that can independently catalyze covalent anchoring of + Braun lipoprotein to peptidoglycan. + - subject: ldt_lpp + predicate: uses acceptor + object: thin_peptidoglycan + description: Lpp-anchoring L,D-transpeptidation uses meso-diaminopimelate in + the peptidoglycan stem peptide as the acceptor for the Lpp C-terminal lysine. + evidence: + - reference: DOI:10.1128/JB.00084-07 + notes: Magnet et al. 2007 mapped the E. coli Lpp-peptidoglycan linkage to the + meso-diaminopimelate residue of a disaccharide-tripeptide muropeptide. + - subject: mature_lpp + predicate: forms + object: lpp_pg_tether + description: Covalent C-terminal linkage to peptidoglycan and N-terminal lipid + anchoring in the outer membrane make Lpp a bridge between the two envelope + layers. + evidence: + - reference: DOI:10.1038/s41467-020-15489-1 + notes: Mathelie-Guinlet and colleagues 2020 measured the contribution of Lpp + outer-membrane-to-peptidoglycan tethers to E. coli envelope stiffness. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-30T19:30:00Z' @@ -69,6 +242,20 @@ curation_history: changes: Added S-BIAD2294 and added exact file 'Figure 3/Replicate 1 (MW240530) 8 minutes/Series002_1.tif', channel 3; per-accession licence, manifest identity, byte count and source taxon mapping verified at import. +- timestamp: '2026-09-04T01:11:45Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph for Gram-negative peptidoglycan outer-membrane tethering, + using additional E. coli Lpp mechanics evidence to explain how the thin wall and + outer membrane are mechanically coupled. + llm_assisted: true +- timestamp: '2026-09-04T04:41:00Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added an ASSEMBLY graph for Lpp maturation, Lol trafficking to the outer + membrane, and L,D-transpeptidase-mediated peptidoglycan tethering; anchored Lpp + nodes with exact UniProt and Pfam identifiers. + llm_assisted: true datasets: - accession: S-BIAD2294 title: Bactericidal Membrane Attack Complex formation initiates at the new pole diff --git a/data/structures/envelope/peptidoglycan_based_cell_wall.yaml b/data/structures/envelope/peptidoglycan_based_cell_wall.yaml index 02bd465..6e7eae6 100644 --- a/data/structures/envelope/peptidoglycan_based_cell_wall.yaml +++ b/data/structures/envelope/peptidoglycan_based_cell_wall.yaml @@ -43,6 +43,115 @@ functions: evidence: - reference: DOI:10.1111/j.1574-6976.2007.00094.x notes: Peptidoglycan structure and architecture. +causal_graphs: +- graph_id: lipid_ii_polymerisation_crosslinking + title: Lipid II flipping, polymerisation and crosslinking build the sacculus + description: The MurJ flippase moves Lipid II from the cytoplasmic leaflet to the + extracytoplasmic face of the cytoplasmic membrane, where SEDS-family RodA/FtsW + polymerases and penicillin-binding transpeptidases turn Lipid II disaccharide-peptide + subunits into crosslinked peptidoglycan strands. The resulting sacculus surrounds + the cell as a covalently closed mesh that bears turgor stress. + graph_kind: ASSEMBLY + scope_status: MECHANISTIC + nodes: + - node_id: lipid_ii + label: Lipid II + node_type: CHEMICAL + grounding: CHEBI:27692 + description: Cytoplasmic-leaflet lipid-linked disaccharide-pentapeptide precursor. + - node_id: murj_flippase + label: MurJ Lipid II flippase + node_type: GENE_OR_PROTEIN + xrefs: + - Pfam:PF03023 + - node_id: exported_lipid_ii + label: extracytoplasmic Lipid II + node_type: CHEMICAL + grounding: CHEBI:27692 + description: Lipid II after translocation to the growth side of the cytoplasmic + membrane. + - node_id: seds_polymerases + label: RodA/FtsW SEDS peptidoglycan polymerases + node_type: GENE_OR_PROTEIN + xrefs: + - InterPro:IPR001182 + - node_id: penicillin_binding_transpeptidases + label: penicillin-binding transpeptidases + node_type: GENE_OR_PROTEIN + xrefs: + - InterPro:IPR001460 + - node_id: glycan_strands + label: alternating GlcNAc-MurNAc glycan strands + node_type: CHEMICAL + - node_id: peptide_crosslinks + label: peptide crosslinks + node_type: CHEMICAL + - node_id: peptidoglycan + label: peptidoglycan + node_type: STRUCTURE + component_ref: peptidoglycan + - node_id: turgor_resistance + label: resistance to turgor pressure + node_type: CAPACITY + edges: + - subject: murj_flippase + predicate: flips + object: exported_lipid_ii + description: MurJ translocates lipid-linked peptidoglycan precursors from the + inner to the outer leaflet of the cytoplasmic membrane so Lipid II is accessible + to extracytoplasmic synthases. + evidence: + - reference: DOI:10.1126/science.1254522 + notes: Sham et al. 2014 showed that E. coli MurJ is needed for Lipid II flipping + during peptidoglycan biogenesis. + - subject: lipid_ii + predicate: supplies + object: exported_lipid_ii + description: Lipid II is the lipid-linked disaccharide-pentapeptide precursor + delivered across the cytoplasmic membrane before polymerisation. + evidence: + - reference: DOI:10.1038/s41579-020-0366-3 + notes: Egan, Errington and Vollmer 2020 review peptidoglycan synthesis from + cytoplasmic lipid-linked precursors through translocation to polymerisation. + - subject: seds_polymerases + predicate: polymerise into + object: glycan_strands + description: RodA and FtsW SEDS proteins polymerise exported Lipid II into glycan + strands for sidewall and septal peptidoglycan assembly. + evidence: + - reference: DOI:10.1038/nmicrobiol.2016.253 + notes: Emami et al. 2017 identified Bacillus subtilis RodA as a peptidoglycan + glycosyltransferase. + - reference: DOI:10.1038/s41564-018-0345-x + notes: Taguchi et al. 2019 reconstituted FtsW peptidoglycan polymerase activity + in complex with its cognate class B penicillin-binding protein. + - subject: penicillin_binding_transpeptidases + predicate: form + object: peptide_crosslinks + description: DD-transpeptidases create peptide bridges between neighboring glycan + strands. + evidence: + - reference: DOI:10.1038/s41579-020-0366-3 + notes: Egan, Errington and Vollmer 2020 review transpeptidation during peptidoglycan + synthesis and remodelling. + - subject: peptide_crosslinks + predicate: connect + object: peptidoglycan + description: Peptide crosslinks turn adjacent glycan chains into a single mesh-like + sacculus. + evidence: + - reference: DOI:10.1111/j.1574-6976.2007.00094.x + notes: Vollmer, Blanot and de Pedro 2008 describe the bacterial sacculus as + glycan strands crosslinked by short peptides. + - subject: peptidoglycan + predicate: resists + object: turgor_resistance + description: The closed, crosslinked sacculus is the stress-bearing layer that + keeps internal turgor pressure from rupturing the cell. + evidence: + - reference: DOI:10.1111/j.1574-6976.2007.00094.x + notes: Vollmer, Blanot and de Pedro 2008 review how peptidoglycan architecture + gives bacteria a protective, shape-maintaining wall. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-30T19:30:00Z' @@ -58,3 +167,17 @@ curation_history: is machine-readable rather than prose. Set per component; ASSOCIATED_MACHINERY only where the protein acts on the already-assembled structure. llm_assisted: true +- timestamp: '2026-09-04T01:12:48Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added an ASSEMBLY graph for Lipid II polymerisation, DD-transpeptidase + crosslinking, and formation of the turgor-resistant peptidoglycan sacculus, with + additional DOI evidence from Egan, Errington and Vollmer 2020. + llm_assisted: true +- timestamp: '2026-09-04T02:27:00Z' + curator: codex + action: REVISE_CAUSAL_GRAPH + changes: Grounded the Lipid II node to ChEBI, anchored MurJ and RodA/FtsW family + nodes to Pfam and InterPro, inserted the MurJ flipping step, and added primary + evidence for RodA and FtsW peptidoglycan polymerase activity. + llm_assisted: true diff --git a/data/structures/envelope/s_layer.yaml b/data/structures/envelope/s_layer.yaml index 6571c5e..e8416d9 100644 --- a/data/structures/envelope/s_layer.yaml +++ b/data/structures/envelope/s_layer.yaml @@ -125,6 +125,10 @@ evidence: causal_graphs: - graph_id: s_layer_self_assembly title: S-layer proteins self-assemble into a surface lattice + description: Secreted S-layer proteins self-assemble into a crystalline two-dimensional + lattice that coats the outer face of the cell. In many Gram-positive S-layers, + SLH domains within the lattice-forming protein bind secondary cell-wall polymers + to retain the lattice on the peptidoglycan-linked envelope surface. graph_kind: ASSEMBLY scope_status: MECHANISTIC nodes: @@ -132,6 +136,14 @@ causal_graphs: label: S-layer (glyco)protein subunit node_type: GENE_OR_PROTEIN component_ref: slp + - node_id: slh_domain + label: S-layer homology domain + node_type: GENE_OR_PROTEIN + component_ref: slh_domain + - node_id: scwp + label: secondary cell-wall polymer + node_type: CHEMICAL + component_ref: scwp - node_id: lattice label: S-layer node_type: STRUCTURE @@ -141,6 +153,15 @@ causal_graphs: label: cell envelope outer surface node_type: CELLULAR_LOCALIZATION edges: + - subject: slh_domain + predicate: is part of + object: slp + description: Tandem SLH domains are N-terminal anchoring modules carried by many + Gram-positive bacterial S-layer proteins. + evidence: + - reference: DOI:10.1038/nrmicro3213 + notes: Fagan and Fairweather 2014 review SLH-domain-mediated anchoring of bacterial + S-layer proteins. - subject: slp predicate: self-assembles into object: lattice @@ -157,6 +178,33 @@ causal_graphs: - reference: DOI:10.1038/nrmicro3213 notes: Fagan and Fairweather 2014 describe bacterial S-layers as cell-surface coats. + - subject: scwp + predicate: localizes to + object: cell_surface + description: In SLH-mediated systems, the secondary cell-wall polymer is linked + to peptidoglycan at the envelope surface. + evidence: + - reference: DOI:10.1111/1574-6976.12063 + notes: Sleytr et al. 2014 review the peptidoglycan-linked secondary cell-wall + polymers that anchor S-layer proteins in many Gram-positive bacteria. + - subject: slh_domain + predicate: binds + object: scwp + description: SLH domains recognize the secondary cell-wall polymer to attach the + S-layer protein to the wall. + evidence: + - reference: DOI:10.1038/nrmicro3213 + notes: Fagan and Fairweather 2014 describe the interaction between SLH domains + and pyruvylated secondary cell-wall polymers. + - subject: scwp + predicate: anchors + object: lattice + description: The SLH-SCWP interaction retains the assembled lattice on the outer + cell-envelope surface. + evidence: + - reference: DOI:10.1038/nrmicro3213 + notes: Fagan and Fairweather 2014 review non-covalent S-layer anchoring through + SLH domains and secondary cell-wall polymers. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-29T00:00:00Z' @@ -192,5 +240,11 @@ curation_history: is machine-readable rather than prose. Set per component; ASSOCIATED_MACHINERY only where the protein acts on the already-assembled structure. llm_assisted: true +- timestamp: '2026-09-04T01:23:31Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Expanded the S-layer assembly graph with SLH-domain and secondary-cell-wall + polymer anchoring nodes and evidence-backed edges. + llm_assisted: true xrefs: - uniprot.location:SL-0262 diff --git a/data/structures/inclusion/gas_vesicle.yaml b/data/structures/inclusion/gas_vesicle.yaml index b2c5993..3b736e0 100644 --- a/data/structures/inclusion/gas_vesicle.yaml +++ b/data/structures/inclusion/gas_vesicle.yaml @@ -62,6 +62,196 @@ evidence: notes: Walsby 1994 comprehensive review. - reference: PMID:22147705 notes: Belenky et al. 2012 structural evidence for the GvpA shell. +causal_graphs: +- graph_id: gvpa_gvpc_buoyancy + title: GvpA and GvpC build gas-filled buoyancy bodies + description: GvpA polymerizes into a ribbed shell around a hollow, gas-filled lumen, + while GvpC reinforces that shell against collapse. The hydrophobic protein wall + excludes liquid water, permits gases to enter, and creates low-density vesicles + that support buoyancy regulation. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: gvpa + label: major gas vesicle protein GvpA + node_type: GENE_OR_PROTEIN + component_ref: gvpa + xrefs: + - Pfam:PF00741 + - node_id: gvpa_shell + label: ribbed GvpA shell + node_type: STRUCTURE + - node_id: gvpc + label: gas vesicle strengthening protein GvpC + node_type: GENE_OR_PROTEIN + component_ref: gvpc + xrefs: + - Pfam:PF01304 + - node_id: gas_vesicle + label: gas vesicle + node_type: STRUCTURE + grounding: GO:0031411 + - node_id: gas_filled_lumen + label: water-excluding gas-filled lumen + node_type: QUALITY + - node_id: buoyancy_regulation + label: buoyancy regulation + node_type: BIOLOGICAL_PROCESS + edges: + - subject: gvpa + predicate: polymerizes into + object: gvpa_shell + description: GvpA subunits assemble into the corrugated protein ribs that form + the gas vesicle wall. + evidence: + - reference: PMID:22147705 + notes: Bayro et al. 2012 used solid-state NMR to support a cross-beta assembly + model for GvpA in gas-vesicle shells. + - reference: DOI:10.1016/j.str.2023.03.011 + notes: Dutka et al. 2023 used cryo-electron tomography of Dolichospermum gas + vesicles to resolve a shell assembled from a helical GvpA filament. + - subject: gvpa_shell + predicate: encloses + object: gas_vesicle + description: The ribbed protein shell forms the hollow cylindrical gas vesicle + body and its conical end caps. + evidence: + - reference: DOI:10.1016/j.str.2023.03.011 + notes: Dutka et al. 2023 resolved the in situ gas-vesicle shell architecture + of Dolichospermum flos-aquae. + - subject: gvpc + predicate: strengthens + object: gvpa_shell + description: GvpC associates with the outside of the GvpA shell and increases + resistance to pressure collapse. + evidence: + - reference: PMID:8177173 + notes: Walsby 1994 reviews experiments showing that GvpC binds the gas vesicle + surface and strengthens cyanobacterial vesicles. + - subject: gvpa_shell + predicate: maintains + object: gas_filled_lumen + description: The hydrophobic shell excludes liquid water while allowing gases + to diffuse across the vesicle wall. + evidence: + - reference: PMID:8177173 + notes: Walsby 1994 reviews the liquid-water impermeability and high gas permeability + of the gas vesicle wall. + - subject: gas_filled_lumen + predicate: enables + object: buoyancy_regulation + description: Retaining gas in many low-density vesicles gives aquatic cells positive + buoyancy for vertical migration. + evidence: + - reference: PMID:8177173 + notes: Walsby 1994 describes how gas vesicles lower cell density and let aquatic + microbes regulate position in the water column. +- graph_id: accessory_gvp_shell_assembly + title: Accessory Gvp interactions scaffold shell assembly + description: Accessory Gvp proteins interact with one another and with the major + shell protein during early gas-vesicle biogenesis. In haloarchaea and the Bacillus + megaterium pNL29 system, GvpF/GvpL-family proteins help connect the hydrophobic + GvpA-family shell subunits with accessory assembly modules that organize growth + of the ribbed gas-vesicle wall. + graph_kind: ASSEMBLY + scope_status: MECHANISTIC + scope_notes: The exact order of gas-vesicle nucleation, cap growth, and cylinder + elongation remains incompletely resolved; this graph captures protein-protein + interaction evidence that supports an accessory-scaffold assembly model. + nodes: + - node_id: gvpf_gvpl + label: GvpF/GvpL-family accessory proteins + node_type: GENE_OR_PROTEIN + xrefs: + - Pfam:PF06386 + - node_id: accessory_gvp_complex + label: accessory Gvp assembly complex + node_type: GENE_OR_PROTEIN + - node_id: gvpa + label: major gas vesicle protein GvpA + node_type: GENE_OR_PROTEIN + component_ref: gvpa + xrefs: + - Pfam:PF00741 + - node_id: gvpa_shell_seed + label: incipient GvpA shell + node_type: STRUCTURE + - node_id: gvpa_shell + label: ribbed GvpA shell + node_type: STRUCTURE + - node_id: gvpc + label: gas vesicle strengthening protein GvpC + node_type: GENE_OR_PROTEIN + component_ref: gvpc + xrefs: + - Pfam:PF01304 + - node_id: gas_vesicle + label: mature gas vesicle + node_type: ORGANELLE + grounding: GO:0031411 + edges: + - subject: gvpf_gvpl + predicate: organize + object: accessory_gvp_complex + description: Haloarchaeal GvpL interacts with multiple accessory Gvp proteins, + while the related GvpF connects to GvpL and additional accessory partners. + evidence: + - reference: DOI:10.3389/fmicb.2020.610179 + notes: Voelkner, Jost and Pfeifer 2020 combined pull-down and split-GFP assays + in Haloferax volcanii to infer a network of interactions among accessory + GvpF-through-GvpM proteins. + - subject: gvpf_gvpl + predicate: recruit + object: gvpa + description: GvpF-family proteins provide an experimentally observed contact + between the accessory assembly network and the major GvpA-family shell protein. + evidence: + - reference: DOI:10.3389/fmicb.2020.610179 + notes: Voelkner, Jost and Pfeifer 2020 mapped GvpF as the sole clear haloarchaeal + accessory-Gvp partner of GvpA in split-GFP tests. + - reference: DOI:10.1038/s44318-024-00178-2 + notes: Iburg et al. 2024 found that the Bacillus megaterium-derived GvpA2/GvpF + contact is masked by other Gvps and reappears when GvpG is removed. + - subject: accessory_gvp_complex + predicate: nucleates + object: gvpa_shell_seed + description: The accessory interaction network is consistent with a transient + complex that controls early GvpA shell nucleation and shields hydrophobic GvpA + surfaces before a hollow wall is established. + evidence: + - reference: DOI:10.3389/fmicb.2020.610179 + notes: Voelkner, Jost and Pfeifer 2020 propose that an accessory-Gvp complex + acts early in gas-vesicle formation and recruits GvpA through GvpF. + - subject: gvpa_shell_seed + predicate: elongates into + object: gvpa_shell + description: A nascent bicone grows as additional GvpA subunits add to the wall + and extend the ribbed shell. + evidence: + - reference: PMID:8177173 + notes: Walsby 1994 reviews the model in which gas-vesicle assembly begins from + small biconical forms that enlarge into the cylindrical vesicle. + - reference: DOI:10.1016/j.str.2023.03.011 + notes: Dutka et al. 2023 resolved the Dolichospermum wall as a helical assembly + of GvpA filaments. + - subject: gvpc + predicate: coats + object: gvpa_shell + description: GvpC is recruited to the outside of the assembled GvpA wall, where + it stabilizes the mature shell against pressure collapse. + evidence: + - reference: PMID:8177173 + notes: Walsby 1994 reviews localization of cyanobacterial GvpC on the outside + of the gas-vesicle shell and its role in shell strengthening. + - subject: gvpa_shell + predicate: matures into + object: gas_vesicle + description: The GvpA wall closes into a hollow, gas-permeable protein organelle + with a water-excluding lumen. + evidence: + - reference: DOI:10.1016/j.str.2023.03.011 + notes: Dutka et al. 2023 show the continuous GvpA-shell architecture of intact + Dolichospermum gas vesicles by cryo-electron tomography. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-30T19:30:00Z' @@ -100,6 +290,20 @@ curation_history: run 14004; required the record's pre-existing exact NCBI taxon and exact GO identity, preserved annotation quality metadata, and stored no imaging volumes. llm_assisted: true +- timestamp: '2026-09-04T01:15:25Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph for GvpA shell formation, GvpC shell strengthening, + liquid-water exclusion, gas retention, and buoyancy regulation, with additional + edge-level use of the Dolichospermum cryo-ET evidence. + llm_assisted: true +- timestamp: '2026-09-04T04:12:00Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added an ASSEMBLY graph for accessory-Gvp interaction networks that recruit + GvpA-family shell proteins, and anchored GvpA, GvpC, and GvpF/GvpL-family graph + nodes with Pfam identifiers. + llm_assisted: true xrefs: - uniprot.location:SL-0125 - MICRO:0000214 diff --git a/data/structures/membrane_organelle/magnetosome.yaml b/data/structures/membrane_organelle/magnetosome.yaml index 111c7f7..f4e1f7b 100644 --- a/data/structures/membrane_organelle/magnetosome.yaml +++ b/data/structures/membrane_organelle/magnetosome.yaml @@ -205,6 +205,7 @@ causal_graphs: - subject: iron predicate: is mineralised into object: crystal + description: Iron imported into the magnetosome vesicle is biomineralised as magnetite. evidence: - reference: DOI:10.1038/nrmicro.2016.99 notes: Uebe & Schüler 2016 describe magnetite biomineralisation within the vesicle. @@ -331,6 +332,11 @@ curation_history: evidence note(s), fetched from PubMed esummary. The notes were previously identical per accession, so a reader could not tell the cited papers apart. Only notes byte-identical to the seeded boilerplate were touched.' +- timestamp: '2026-09-04T01:40:08Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Added the missing description to the magnetosome iron-mineralisation edge. + llm_assisted: true xrefs: - uniprot.location:SL-0510 - MICRO:0000216 diff --git a/data/structures/microcompartment/carboxysome.yaml b/data/structures/microcompartment/carboxysome.yaml index 9622aff..370d87f 100644 --- a/data/structures/microcompartment/carboxysome.yaml +++ b/data/structures/microcompartment/carboxysome.yaml @@ -561,6 +561,8 @@ causal_graphs: - subject: shell predicate: permits passage of object: bicarbonate + description: Selective shell pores admit cytosolic bicarbonate into the carboxysome + lumen. evidence: - reference: DOI:10.1038/nrmicro.2018.10 notes: Shell pores are selective for small anions such as HCO3-. @@ -574,18 +576,24 @@ causal_graphs: - subject: ca predicate: elevates local concentration of object: co2 + description: Carbonic anhydrase enriches CO2 inside the shell by dehydrating imported + bicarbonate. evidence: - reference: DOI:10.1128/MMBR.00061-12 notes: Rae et al. 2013. - subject: shell predicate: prevents loss of object: co2 + description: The protein shell slows CO2 leakage to retain substrate near the + encapsulated RuBisCO. evidence: - reference: DOI:10.1038/nrmicro.2018.10 notes: The shell retards CO2 efflux to the cytoplasm. - subject: co2 predicate: substrate of object: rubisco + description: Locally generated CO2 is the carboxylation substrate for RuBisCO + inside the carboxysome. evidence: - reference: DOI:10.1128/MMBR.00061-12 notes: Rae et al. 2013. @@ -593,6 +601,7 @@ causal_graphs: predicate: catalyses object: fixation predicate_id: RO:0002327 + description: Encapsulated RuBisCO fixes CO2 into the Calvin-Benson-Bassham cycle. evidence: - reference: DOI:10.1128/MMBR.00061-12 notes: Rae et al. 2013. @@ -650,6 +659,8 @@ causal_graphs: - subject: scaffold predicate: forms object: procarboxysome + description: Scaffolded RuBisCO condenses before shell recruitment to create the + beta-carboxysome precursor. evidence: - reference: DOI:10.1128/MMBR.00061-12 notes: Rae et al. 2013 describe cargo condensation preceding shell encapsulation @@ -683,12 +694,15 @@ causal_graphs: - subject: bmc_h predicate: forms object: shell + description: BMC-H hexamers tile the flat facets of the carboxysome shell. evidence: - reference: DOI:10.1038/nrmicro.2018.10 notes: Kerfeld et al. 2018 describe BMC-H hexamers tiling the shell facets. - subject: bmc_t predicate: forms object: shell + description: CcmP-family BMC-T proteins contribute stacked trimer pseudohexamers + to the shell. evidence: - reference: PMID:23572529 notes: UniProt cites this paper (Q31QW7) for CcmP forming a dimer of stacked @@ -696,6 +710,7 @@ causal_graphs: - subject: shell predicate: encapsulates object: procarboxysome + description: Shell facets assemble around the condensed cargo to close the carboxysome. evidence: - reference: DOI:10.1128/MMBR.00061-12 notes: Rae et al. 2013 describe the shell closing around the condensed cargo. @@ -804,6 +819,11 @@ curation_history: evidence note(s), fetched from PubMed esummary. The notes were previously identical per accession, so a reader could not tell the cited papers apart. Only notes byte-identical to the seeded boilerplate were touched.' +- timestamp: '2026-09-04T01:40:08Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Added descriptions to the remaining carboxysome CO2-concentrating and assembly + graph edges so every causal edge now states its mechanism. xrefs: - uniprot.location:SL-0034 discussions: diff --git a/data/structures/microcompartment/encapsulin_nanocompartment.yaml b/data/structures/microcompartment/encapsulin_nanocompartment.yaml index 752b3ec..fd06dd5 100644 --- a/data/structures/microcompartment/encapsulin_nanocompartment.yaml +++ b/data/structures/microcompartment/encapsulin_nanocompartment.yaml @@ -95,6 +95,190 @@ evidence: - reference: DOI:10.1038/nmicrobiol.2017.29 notes: '''Widespread distribution of encapsulin nanocompartments reveals functional diversity'', Nature Microbiology 2017.' +causal_graphs: +- graph_id: cargo_targeting_iron_storage + title: Targeting peptides load iron-mineralising cargo into the shell + description: Encapsulin shell proteins self-assemble into HK97-fold icosahedra, + and C-terminal targeting peptides load ferritin-like cargo proteins onto the shell + interior. The enclosed cargo oxidises and mineralises iron inside the nanocompartment, + storing iron away from the cytosol to buffer iron and oxidative stress. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: shell + label: encapsulin shell protein + node_type: GENE_OR_PROTEIN + component_ref: shell + xrefs: + - Pfam:PF04454 + - node_id: cargo + label: targeted ferritin-like cargo enzymes + node_type: GENE_OR_PROTEIN + component_ref: cargo + - node_id: encapsulin_shell + label: encapsulin nanocompartment + node_type: STRUCTURE + grounding: GO:0140737 + - node_id: ferrous_iron + label: ferrous iron + node_type: CHEMICAL + grounding: CHEBI:29033 + - node_id: ferric_mineral_core + label: ferric mineral core + node_type: CHEMICAL + - node_id: iron_stress_buffering + label: iron and oxidative-stress buffering + node_type: CAPACITY + edges: + - subject: shell + predicate: self-assembles into + object: encapsulin_shell + description: Encapsulin shell protomers assemble into thin icosahedral protein + cages. + evidence: + - reference: DOI:10.1038/nsmb.1473 + notes: Sutter et al. 2008 resolved a Thermotoga maritima encapsulin shell made + from 60 shell-protein copies. + - reference: DOI:10.1016/j.cbpa.2016.05.013 + notes: Giessen 2016 reviews HK97-fold encapsulin shell assembly in T=1 and T=3 + architectures. + - subject: cargo + predicate: binds + object: shell + description: C-terminal targeting peptides on cargo enzymes bind the shell interior + and direct cargo loading. + evidence: + - reference: DOI:10.1038/nsmb.1473 + notes: Sutter et al. 2008 identified conserved binding sites inside the shell + for short C-terminal targeting peptides on oxidative-stress enzymes. + - reference: DOI:10.1038/s41598-021-84329-z + notes: Altenburg et al. 2021 dissected hydrophobic and ionic interactions + that govern targeting-peptide binding to Thermotoga maritima and Myxococcus + xanthus encapsulin shells. + - subject: encapsulin_shell + predicate: encloses + object: cargo + description: The closed shell packages ferritin-like enzymes and separates their + iron chemistry from the surrounding cytosol. + evidence: + - reference: DOI:10.15252/embj.201488566 + notes: McHugh et al. 2014 showed that Myxococcus xanthus encapsulin shells are + lined with ferritin-like adaptor proteins that nucleate iron-rich granules. + - subject: cargo + predicate: mineralises + object: ferrous_iron + description: Encapsulated ferritin-like cargo oxidises Fe2+ and drives ferric + mineral deposition in the lumen. + evidence: + - reference: DOI:10.15252/embj.201488566 + notes: McHugh et al. 2014 linked ferritin-like encapsulin cargoes with iron + sequestration inside the protein shell. + - subject: ferrous_iron + predicate: becomes + object: ferric_mineral_core + description: Ferrous iron is converted into a sequestered iron-rich mineral core + inside the nanocompartment. + evidence: + - reference: DOI:10.15252/embj.201488566 + notes: McHugh et al. 2014 observed dense iron-rich cores in native Myxococcus + xanthus encapsulins. + - subject: ferric_mineral_core + predicate: buffers + object: iron_stress_buffering + description: Internal mineralisation stores iron away from the cytosol and protects + cells from iron starvation and oxidative stress. + evidence: + - reference: DOI:10.15252/embj.201488566 + notes: McHugh et al. 2014 tied the Myxococcus xanthus encapsulin system to iron + storage and oxidative-stress protection. +- graph_id: hk97_targeting_peptide_shell_assembly + title: HK97-fold shells assemble around peptide-tagged cargo + description: Type 1 encapsulin shell protomers form HK97-fold icosahedral cages. + Short cargo targeting peptides bind pockets on the shell interior during assembly, + producing a closed nanocompartment that selectively encloses enzyme cargo. + graph_kind: ASSEMBLY + scope_status: MECHANISTIC + nodes: + - node_id: shell + label: encapsulin shell protein + node_type: GENE_OR_PROTEIN + component_ref: shell + xrefs: + - Pfam:PF04454 + - node_id: hk97_protomer + label: HK97-fold shell protomer + node_type: STRUCTURE + - node_id: targeting_peptide + label: C-terminal cargo targeting peptide + node_type: GENE_OR_PROTEIN + - node_id: cargo + label: targeted cargo enzymes + node_type: GENE_OR_PROTEIN + component_ref: cargo + - node_id: interior_binding_pocket + label: shell-interior peptide binding pocket + node_type: STRUCTURE + - node_id: cargo_loaded_shell + label: cargo-loaded encapsulin shell + node_type: STRUCTURE + grounding: GO:0140737 + edges: + - subject: shell + predicate: folds as + object: hk97_protomer + description: Encapsulin shell proteins adopt an HK97-like fold that is reused + by many viral capsid proteins. + evidence: + - reference: DOI:10.1038/nsmb.1473 + notes: Sutter et al. 2008 resolved the Thermotoga maritima encapsulin shell + and found an HK97-like shell-protein fold. + - subject: hk97_protomer + predicate: self-assembles into + object: cargo_loaded_shell + description: Shell protomers self-assemble into icosahedral cages that can form + without cargo and package cargo when targeting peptides are present. + evidence: + - reference: DOI:10.15252/embj.201488566 + notes: McHugh et al. 2014 resolved the 180-subunit Myxococcus xanthus EncA + shell and its ferritin-like cargo. + - reference: DOI:10.1016/j.cbpa.2016.05.013 + notes: Giessen 2016 reviews T=1 and T=3 encapsulin shell architectures. + - subject: cargo + predicate: exposes + object: targeting_peptide + description: Encapsulin cargo proteins carry terminal peptide tags that are + sufficient to route native or heterologous proteins into the assembling shell. + evidence: + - reference: DOI:10.1021/acs.biochem.6b00294 + notes: Cassidy-Amstutz et al. 2016 identified minimal peptide tags that load + proteins into Thermotoga maritima encapsulins in vivo and in vitro. + - subject: targeting_peptide + predicate: binds + object: interior_binding_pocket + description: Hydrophobic and ionic contacts between targeting peptides and the + shell interior determine shell binding strength and cargo-loading specificity. + evidence: + - reference: DOI:10.1038/s41598-021-84329-z + notes: Altenburg et al. 2021 characterized and engineered targeting-peptide + interactions with Thermotoga maritima and Myxococcus xanthus shell interiors. + - subject: interior_binding_pocket + predicate: recruits + object: cargo + description: Binding sites on the inner shell surface capture targeting peptides + and localize cargo enzymes into the nascent shell lumen. + evidence: + - reference: DOI:10.1038/nsmb.1473 + notes: Sutter et al. 2008 identified conserved binding sites for targeting + peptides on the inside of the Thermotoga maritima shell. + - subject: cargo_loaded_shell + predicate: encloses + object: cargo + description: Completion of the shell leaves the targeted enzymes packaged inside + the encapsulin lumen. + evidence: + - reference: DOI:10.15252/embj.201488566 + notes: McHugh et al. 2014 showed ferritin-like cargoes enclosed inside native + Myxococcus xanthus encapsulin shells. mapping_status: PROPOSED curation_history: - timestamp: '2026-09-02T04:49:54Z' @@ -103,3 +287,17 @@ curation_history: changes: Drafted from the cited reviews; every GO term, taxon id and DOI resolved live before writing. Not yet human-reviewed. llm_assisted: true +- timestamp: '2026-09-04T01:17:11Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph for targeting-peptide cargo loading and ferritin-like + iron mineralisation inside encapsulin shells, with primary evidence from Sutter + et al. 2008 and McHugh et al. 2014. + llm_assisted: true +- timestamp: '2026-09-04T04:22:00Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added an ASSEMBLY graph for HK97-fold shell self-assembly around + targeting-peptide-tagged cargo, grounded ferrous iron with ChEBI, and anchored + shell protein nodes with Pfam. + llm_assisted: true diff --git a/data/structures/nucleoid/nucleoid.yaml b/data/structures/nucleoid/nucleoid.yaml index 85d5ed3..fdc7153 100644 --- a/data/structures/nucleoid/nucleoid.yaml +++ b/data/structures/nucleoid/nucleoid.yaml @@ -49,6 +49,94 @@ functions: evidence: - reference: DOI:10.1038/nrmicro2261 notes: Bacterial nucleoid-associated proteins, nucleoid structure and gene expression. +- reference: DOI:10.1371/journal.pgen.1008456 + notes: Verma, Qian and Adhya 2019 review multiscale Escherichia coli nucleoid architecture. +causal_graphs: +- graph_id: nap_supercoiling_chromosome_compaction + title: NAPs and supercoils compact DNA into an organized nucleoid + description: Nucleoid-associated proteins bind the bacterial chromosome and alter + its local geometry by bending, wrapping, bridging, and constraining DNA. These + local nucleoprotein states combine with plectonemic supercoils and topological + domains to compact the chromosome into a dynamic nucleoid that still supports + DNA replication and transcription. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: chromosomal_dna + label: chromosomal DNA + node_type: GENETIC_ELEMENT + component_ref: chromosomal_dna + - node_id: nucleoid_associated_proteins + label: nucleoid-associated proteins + node_type: GENE_OR_PROTEIN + component_ref: nucleoid_associated_proteins + - node_id: local_dna_bridging + label: locally bent and bridged DNA + node_type: STATE + - node_id: plectonemic_supercoils + label: plectonemic supercoiled loops + node_type: STATE + - node_id: nucleoid + label: nucleoid + node_type: STRUCTURE + grounding: GO:0009295 + - node_id: chromosome_organization + label: chromosome organization + node_type: BIOLOGICAL_PROCESS + grounding: GO:0051276 + edges: + - subject: nucleoid_associated_proteins + predicate: bind + object: chromosomal_dna + description: NAPs bind the bacterial chromosome at abundant specific and nonspecific + sites. + evidence: + - reference: DOI:10.1038/nrmicro2261 + notes: Dillon and Dorman 2010 review NAP binding across the bacterial chromosome. + - subject: nucleoid_associated_proteins + predicate: bend and bridge + object: local_dna_bridging + description: NAPs bend, wrap, bridge, and bunch DNA at the sub-kilobase scale. + evidence: + - reference: DOI:10.1371/journal.pgen.1008456 + notes: Verma, Qian and Adhya 2019 review DNA bending, looping, bridging and + wrapping by nucleoid-associated architectural proteins. + - subject: local_dna_bridging + predicate: constrains + object: plectonemic_supercoils + description: Architectural proteins constrain negative supercoils and help partition + chromosomal DNA into topological loops. + evidence: + - reference: DOI:10.1371/journal.pgen.1008456 + notes: Verma, Qian and Adhya 2019 describe NAP constraint of negative supercoils + as a route to chromosome topological organization. + - subject: chromosomal_dna + predicate: folds into + object: plectonemic_supercoils + description: Supercoiling folds the chromosome into plectonemic loops at the tens-of-kilobases + scale. + evidence: + - reference: DOI:10.1371/journal.pgen.1008456 + notes: Verma, Qian and Adhya 2019 describe larger bacterial chromosome loops + as plectonemic forms induced by supercoiling. + - subject: plectonemic_supercoils + predicate: compact into + object: nucleoid + description: Plectonemic loops and longer-range contacts coalesce into a compact, + spatially organized nucleoid. + evidence: + - reference: DOI:10.1371/journal.pgen.1008456 + notes: Verma, Qian and Adhya 2019 review hierarchical compaction of E. coli + chromosomal DNA into spatial domains and the nucleoid. + - subject: nucleoid + predicate: organizes + object: chromosome_organization + description: The final folded nucleoid keeps the chromosome condensed while leaving + DNA accessible for replication, transcription, and segregation. + evidence: + - reference: DOI:10.1038/nrmicro2261 + notes: Dillon and Dorman 2010 review the dynamic coupling of bacterial nucleoid + structure with gene expression. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-30T19:30:00Z' @@ -69,5 +157,12 @@ curation_history: is machine-readable rather than prose. Set per component; ASSOCIATED_MACHINERY only where the protein acts on the already-assembled structure. llm_assisted: true +- timestamp: '2026-09-04T01:18:32Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph for NAP-mediated DNA binding, bending, bridging, + supercoil constraint, and multiscale chromosomal compaction into the nucleoid, + with additional evidence from Verma, Qian and Adhya 2019. + llm_assisted: true xrefs: - uniprot.location:SL-0187 diff --git a/data/structures/other/methyl_accepting_chemotaxis_protein_complex.yaml b/data/structures/other/methyl_accepting_chemotaxis_protein_complex.yaml index 7362629..2d5f370 100644 --- a/data/structures/other/methyl_accepting_chemotaxis_protein_complex.yaml +++ b/data/structures/other/methyl_accepting_chemotaxis_protein_complex.yaml @@ -135,7 +135,114 @@ curation_history: is no curation reason to differ -- the exception list is for residuals a curator has accepted, not for making a gate quiet.' llm_assisted: true +- timestamp: '2026-09-04T04:32:00Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Added a CheA/CheW ASSEMBLY graph for hexagonal array formation, anchored + MCP and CheW graph nodes with Pfam identifiers, added a directly cited + CheA-to-CheY phosphotransfer edge, and resolved the phosphotransfer curation + TODO. + llm_assisted: true causal_graphs: +- graph_id: chea_chew_hexagonal_array_assembly + title: CheA and CheW network receptor trimers into a hexagonal array + description: Methyl-accepting chemotaxis proteins assemble as receptor trimers of + dimers. CheA dimers and CheW couplers connect neighboring trimers through a baseplate + of alternating CheA regulatory domains and CheW subunits, yielding the extended + hexagonal array that supports cooperative chemotaxis signalling. + graph_kind: ASSEMBLY + scope_status: MECHANISTIC + nodes: + - node_id: mcp + label: methyl-accepting chemotaxis protein + node_type: GENE_OR_PROTEIN + component_ref: mcp + xrefs: + - Pfam:PF00015 + - node_id: receptor_trimer + label: MCP trimer of dimers + node_type: STRUCTURE + - node_id: chea + label: CheA histidine kinase dimer + node_type: GENE_OR_PROTEIN + component_ref: chea + - node_id: chew + label: CheW coupling protein + node_type: GENE_OR_PROTEIN + component_ref: chew + xrefs: + - Pfam:PF01584 + - node_id: chea_chew_ring + label: alternating CheA/CheW baseplate ring + node_type: STRUCTURE + - node_id: core_signaling_unit + label: chemoreceptor core signaling unit + node_type: STRUCTURE + - node_id: array + label: methyl accepting chemotaxis protein complex + node_type: STRUCTURE + grounding: GO:0098561 + edges: + - subject: mcp + predicate: oligomerizes into + object: receptor_trimer + description: Chemoreceptor dimers are organized as trimers of dimers at vertices + of the lattice. + evidence: + - reference: DOI:10.1073/pnas.1115719109 + notes: Briegel et al. 2012 combined crystallography with cryo-electron + tomography of native arrays to place receptor trimers of dimers at hexagonal + lattice vertices. + - subject: chea + predicate: bridges + object: receptor_trimer + description: One CheA dimer connects two receptor trimers as part of the core + chemotaxis signaling unit. + evidence: + - reference: DOI:10.1073/pnas.1104824108 + notes: Li and Hazelbauer 2011 showed that purified core signaling complexes + contained two receptor trimers of dimers and two CheW proteins for each CheA + dimer. + - subject: chew + predicate: couples + object: receptor_trimer + description: CheW links receptor trimers to CheA and helps build the repeating + core signaling unit. + evidence: + - reference: DOI:10.1073/pnas.1104824108 + notes: Li and Hazelbauer 2011 established the two-CheW stoichiometry of the + two-trimer, one-CheA-dimer core unit. + - subject: receptor_trimer + predicate: combines with + object: chea_chew_ring + description: Receptor trimer vertices surround rings of alternating CheA P5 + regulatory domains and CheW couplers. + evidence: + - reference: DOI:10.1073/pnas.1115719109 + notes: Briegel et al. 2012 modeled the receptor trimers surrounding alternating + CheA/CheW rings in the cytoplasmic baseplate. + - subject: chea_chew_ring + predicate: forms + object: core_signaling_unit + description: The CheA/CheW ring and associated receptor trimers define the repeated + building block of the chemoreceptor array. + evidence: + - reference: DOI:10.1021/bi5000614 + notes: Briegel, Li, Bilwes, Hughes, Jensen and Crane 2014 reviewed a sequential + assembly model in which two receptor trimers, one CheA dimer, and two CheW + monomers form the core functional unit before hexagons and the superlattice. + - subject: core_signaling_unit + predicate: tiles into + object: array + description: Core units share CheA/CheW linkers to produce the extended hexagonal + chemotaxis array with conserved 12 nm spacing. + evidence: + - reference: DOI:10.1073/pnas.0905181106 + notes: Briegel et al. 2009 found a conserved hexagonal lattice spacing of about + 12 nm in chemoreceptor arrays from diverse bacteria and archaea. + - reference: DOI:10.1073/pnas.1115719109 + notes: Briegel et al. 2012 showed that CheA dimerization domains link neighboring + rings to form the extended stable array. - graph_id: chemoreceptor_array_signalling title: Chemoeffector binding is amplified by the array and read out as phospho-CheY description: 'The array''s function is gain: binding at one receptor reaches ~35 @@ -153,10 +260,14 @@ causal_graphs: label: methyl-accepting chemotaxis protein node_type: GENE_OR_PROTEIN component_ref: mcp + xrefs: + - Pfam:PF00015 - node_id: chew label: CheW coupling protein node_type: GENE_OR_PROTEIN component_ref: chew + xrefs: + - Pfam:PF01584 - node_id: chea label: CheA histidine autokinase node_type: GENE_OR_PROTEIN @@ -232,6 +343,16 @@ causal_graphs: notes: Verbatim. Stated as an implication of the observations, not a direct measurement, and the edge is no stronger than that. The CheA-to-CheY phosphotransfer step is not stated quotably in this source, so it is not drawn as an edge. + - subject: chea + predicate: transfers phosphoryl group to + object: phospho_chey + description: Autophosphorylated CheA binds CheY and transfers its phosphoryl + group to generate the phospho-CheY signal read by the flagellar motor. + evidence: + - reference: DOI:10.1021/bi962261k + notes: Stewart 1997 kinetically characterized CheA-to-CheY phosphotransfer + as reversible CheY binding to phospho-CheA followed by rapid reversible + phosphoryl transfer. - subject: phospho_chey predicate: signals object: motor_reversal @@ -252,10 +373,13 @@ discussions: a primary source for the phosphotransfer be added, or is the array's output adequately described by 'the receptor cluster produces phospho-CheY signals'? kind: CURATION_TODO - status: OPEN + status: RESOLVED attaches_to: - causal_graphs#chemoreceptor_array_signalling rationale: 'The graph deliberately stops where the source stops. Drawing the step from background knowledge would be the defect #161 records.' + resolution_note: Added an evidence-backed CheA-to-phospho-CheY edge from the Stewart + 1997 kinetic characterization of CheA-to-CheY phosphotransfer. posed_by: claude + resolved_date: '2026-09-04' posed_date: '2026-09-02' diff --git a/data/structures/ribonucleoprotein/ribosome.yaml b/data/structures/ribonucleoprotein/ribosome.yaml index cd97a8b..1facddd 100644 --- a/data/structures/ribonucleoprotein/ribosome.yaml +++ b/data/structures/ribonucleoprotein/ribosome.yaml @@ -269,6 +269,8 @@ causal_graphs: - subject: aa_trna predicate: substrate of object: peptide_bond + description: The A-site aminoacyl-tRNA supplies the amino group used to form the + next peptide bond. evidence: - reference: DOI:10.1038/nature08403 notes: Aminoacyl-tRNA in the A site donates its amino group to the peptidyl-tRNA @@ -294,6 +296,8 @@ causal_graphs: predicate: occurs in object: ribosome predicate_id: BFO:0000066 + description: After peptidyl transfer, EF-G accelerates ribosomal movement of tRNAs + and mRNA by one codon. evidence: - reference: DOI:10.1038/nature08403 notes: Translocation is an intrinsic ribosomal motion accelerated by EF-G. @@ -409,6 +413,12 @@ curation_history: caption states that instead of letting the composite read as a micrograph. Taxon NCBITaxon:83333 was already a canonical example on the record.' llm_assisted: true +- timestamp: '2026-09-04T01:40:08Z' + curator: codex + action: ENHANCE_CAUSAL_GRAPH + changes: Added descriptions to the remaining ribosome elongation-cycle edges so + every edge now states the substrate or translocation step it represents. + llm_assisted: true complex_compositions: - composition_id: complex_portal_cpx_3802 source: COMPLEX_PORTAL diff --git a/data/structures/secretion_system/type_iii_protein_secretion_system_complex.yaml b/data/structures/secretion_system/type_iii_protein_secretion_system_complex.yaml index c4166fb..aa4043e 100644 --- a/data/structures/secretion_system/type_iii_protein_secretion_system_complex.yaml +++ b/data/structures/secretion_system/type_iii_protein_secretion_system_complex.yaml @@ -125,6 +125,102 @@ evidence: - reference: DOI:10.1016/j.cell.2018.01.034 notes: Galan JE & Waksman G 2018, 'Protein-Injection Machines in Bacteria', Cell — independent review covering the injectisome alongside the other injection systems. +causal_graphs: +- graph_id: export_gate_needle_translocon_injection + title: The export gate feeds unfolded effectors into a host-cell conduit + description: Inner- and outer-membrane rings align the export apparatus with the + needle filament, creating a conduit through the bacterial envelope. The export + gate recognizes unfolded substrates, the narrow needle conducts them away from + the basal body, and the translocon completes the channel in the target-cell membrane. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: secretin + label: outer-membrane secretin ring + node_type: GENE_OR_PROTEIN + component_ref: secretin + - node_id: inner_rings + label: inner-membrane rings + node_type: GENE_OR_PROTEIN + component_ref: inner_rings + - node_id: export_apparatus + label: export apparatus + node_type: GENE_OR_PROTEIN + component_ref: export_apparatus + - node_id: needle + label: needle filament + node_type: GENE_OR_PROTEIN + component_ref: needle + - node_id: translocon + label: translocon pore + node_type: GENE_OR_PROTEIN + component_ref: translocon + - node_id: translocation_conduit + label: continuous effector conduit + node_type: STRUCTURE + grounding: GO:0030257 + - node_id: unfolded_effectors + label: unfolded effector proteins + node_type: GENE_OR_PROTEIN + - node_id: t3ss_secretion + label: protein secretion by the type III secretion system + node_type: BIOLOGICAL_PROCESS + grounding: GO:0030254 + edges: + - subject: inner_rings + predicate: align + object: export_apparatus + description: The inner-membrane rings organize the basal body around the membrane + export apparatus. + evidence: + - reference: DOI:10.1038/nrmicro.2017.20 + notes: Deng et al. 2017 review the export apparatus within the inner rings of + the injectisome basal body. + - subject: secretin + predicate: extends + object: translocation_conduit + description: The secretin ring supplies the outer-membrane channel of the basal + body. + evidence: + - reference: DOI:10.1038/nrmicro.2017.20 + notes: Deng et al. 2017 describe the outer-membrane secretin as part of the + envelope-spanning basal body. + - subject: export_apparatus + predicate: exports + object: unfolded_effectors + description: The export apparatus gates type III substrates and exports them in + an unfolded state. + evidence: + - reference: DOI:10.1016/j.cell.2018.01.034 + notes: Galan and Waksman 2018 describe unfolded substrates passing through the + type III needle conduit. + - subject: needle + predicate: extends + object: translocation_conduit + description: The helical needle filament forms the narrow channel that carries + unfolded effectors beyond the bacterial surface. + evidence: + - reference: DOI:10.1016/j.cell.2018.01.034 + notes: Galan and Waksman 2018 report a helical needle filament enclosing an + inner channel that conducts unfolded substrates. + - subject: translocon + predicate: completes + object: translocation_conduit + description: Translocon proteins insert in the host membrane and connect the injectisome + channel to the host cytosol. + evidence: + - reference: DOI:10.1038/nrmicro.2017.20 + notes: Deng et al. 2017 review translocon insertion into the host membrane during + one-step effector translocation. + - subject: translocation_conduit + predicate: delivers + object: t3ss_secretion + description: The assembled conduit exports effector proteins directly from the + bacterial cytoplasm into the eukaryotic host cell. + evidence: + - reference: DOI:10.1038/nrmicro.2017.20 + notes: Deng et al. 2017 review injectisome-mediated one-step effector delivery + from bacteria into host cells. mapping_status: PROPOSED curation_history: - timestamp: '2026-08-31T03:48:12Z' @@ -198,6 +294,12 @@ curation_history: is restored verbatim. The narrowing moves to `notes`, and posed_date returns to when the question was actually raised.' llm_assisted: true +- timestamp: '2026-09-04T01:20:09Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph for type III export through the basal body, export + apparatus, needle filament, and host-membrane translocon. + llm_assisted: true xrefs: - GO:0009288 discussions: diff --git a/data/structures/spore/endospore_external_encapsulating_structure.yaml b/data/structures/spore/endospore_external_encapsulating_structure.yaml index 520c6b6..1e73b1a 100644 --- a/data/structures/spore/endospore_external_encapsulating_structure.yaml +++ b/data/structures/spore/endospore_external_encapsulating_structure.yaml @@ -125,6 +125,175 @@ evidence: assembly and functions of the multilayered coat'', Nature Reviews Microbiology.' - reference: DOI:10.1128/9781555819323.ch10 notes: '''Spore Resistance Properties'', in The Bacterial Spore (2016).' +causal_graphs: +- graph_id: spoiva_cote_coat_assembly + title: SpoIVA and CotE organize spore coat layer assembly + description: SpoIVA self-assembly creates the basement scaffold that anchors early + coat morphogenesis around the forespore. CotE then localizes outside that inner + scaffold and organizes assembly of the outer Bacillus subtilis spore coat. + graph_kind: ASSEMBLY + scope_status: MECHANISTIC + nodes: + - node_id: spoiva + label: SpoIVA + node_type: GENE_OR_PROTEIN + xrefs: + - UniProtKB:P35149 + - node_id: basement_layer + label: spore coat basement layer + node_type: STRUCTURE + - node_id: inner_coat + label: inner spore coat + node_type: STRUCTURE + - node_id: cote + label: CotE + node_type: GENE_OR_PROTEIN + xrefs: + - UniProtKB:P14016 + - node_id: outer_coat + label: outer spore coat + node_type: STRUCTURE + - node_id: multilayered_coat + label: endospore coat + node_type: STRUCTURE + grounding: GO:0043593 + edges: + - subject: spoiva + predicate: self-assembles into + object: basement_layer + description: SpoIVA binds and hydrolyses ATP and self-assembles into higher-order + polymers that build the innermost basement coat layer. + evidence: + - reference: DOI:10.1016/j.molcel.2008.05.030 + notes: Ramamurthi and Losick 2008 reconstituted ATP-driven SpoIVA self-assembly + into cable-like higher-order structures. + - subject: basement_layer + predicate: recruits + object: inner_coat + description: The basement layer on the forespore surface provides the scaffold + on which inner-coat proteins assemble. + evidence: + - reference: DOI:10.1101/gad.8.2.234 + notes: Driks et al. 1994 localized key coat proteins and proposed that SpoIVA + creates the basement layer used for coat assembly. + - subject: inner_coat + predicate: positions + object: cote + description: CotE is recruited after early inner-coat morphogenesis and marks + the future outer-coat layer. + evidence: + - reference: DOI:10.1038/nrmicro2921 + notes: McKenney, Driks and Eichenberger 2012 review CotE as a morphogenetic + organizer assembled outside the inner coat. + - subject: cote + predicate: organizes + object: outer_coat + description: CotE is required to organize outer coat proteins into the outer layer. + evidence: + - reference: PMID:3139490 + notes: Zheng et al. identified CotE as a morphogenetic protein required for + outer Bacillus subtilis coat assembly. + - subject: outer_coat + predicate: layers with + object: multilayered_coat + description: Inner and outer coat morphogenetic modules yield the mature layered + endospore coat that surrounds the cortex. + evidence: + - reference: DOI:10.1038/nrmicro2921 + notes: McKenney, Driks and Eichenberger 2012 review the basement, inner, outer + and crust layers that make up the Bacillus subtilis spore coat. +- graph_id: cortex_coat_resistance + title: Cortex dehydration and coat barriers make spores stress resistant + description: The chemically modified cortex is the peptidoglycan layer that maintains + a dehydrated spore core, and dehydration is a major source of wet-heat resistance. + Outside the cortex, morphogenetic coat proteins assemble dozens of proteins into + a multilayered shell that blocks lytic enzymes and large toxic molecules. + graph_kind: FUNCTION + scope_status: MECHANISTIC + nodes: + - node_id: cortex + label: endospore cortex peptidoglycan + node_type: STRUCTURE + grounding: GO:0043595 + component_ref: cortex + - node_id: coat + label: endospore coat proteins + node_type: GENE_OR_PROTEIN + component_ref: coat + - node_id: dehydrated_core + label: dehydrated spore core + node_type: STATE + - node_id: multilayered_coat + label: multilayered spore coat + node_type: STRUCTURE + grounding: GO:0043593 + - node_id: coat_barrier + label: enzyme and toxin barrier + node_type: CAPACITY + - node_id: spore_resistance + label: spore-mediated stress resistance + node_type: CAPACITY + - node_id: external_structure + label: endospore external encapsulating structure + node_type: STRUCTURE + grounding: GO:0043591 + edges: + - subject: cortex + predicate: maintains + object: dehydrated_core + description: Modified cortex peptidoglycan keeps the spore core dehydrated. + evidence: + - reference: DOI:10.1128/9781555819323.ch10 + notes: Setlow 2016 reviews the cortex contribution to spore core dehydration + and wet-heat resistance. + - subject: dehydrated_core + predicate: enables + object: spore_resistance + description: Core dehydration is a major physical basis for endospore resistance + to wet heat. + evidence: + - reference: DOI:10.1128/9781555819323.ch10 + notes: Setlow 2016 reviews low core water content as a determinant of spore + wet-heat resistance. + - subject: coat + predicate: assembles into + object: multilayered_coat + description: SpoIVA, SafA, CotE and other morphogenetic proteins organize coat + proteins into the layered shell outside the cortex. + evidence: + - reference: DOI:10.1038/nrmicro2921 + notes: McKenney, Driks and Eichenberger 2012 review the morphogenetic hierarchy + that builds Bacillus subtilis spore coat layers. + - reference: PMID:3139490 + notes: Zheng et al. identified CotE as a morphogenetic protein required for + outer Bacillus subtilis coat assembly. + - subject: multilayered_coat + predicate: forms + object: external_structure + description: The mature protein coat is one of the external layers surrounding + the cortex and dehydrated core. + evidence: + - reference: DOI:10.1038/nrmicro2921 + notes: McKenney, Driks and Eichenberger 2012 review the spore coat as a multilayered + shell outside the cortex. + - subject: multilayered_coat + predicate: excludes + object: coat_barrier + description: The coat restricts access of lytic enzymes and large toxic molecules + to the spore interior. + evidence: + - reference: DOI:10.1038/nrmicro2921 + notes: McKenney, Driks and Eichenberger 2012 describe the coat as a barrier + against lytic enzymes and large toxic molecules. + - subject: coat_barrier + predicate: contributes to + object: spore_resistance + description: Surface-layer exclusion complements cortex-driven core dehydration + to protect the dormant spore. + evidence: + - reference: DOI:10.1128/9781555819323.ch10 + notes: Setlow 2016 reviews spore resistance properties contributed by external + endospore structures. mapping_status: PROPOSED curation_history: - timestamp: '2026-09-01T03:41:49Z' @@ -142,3 +311,16 @@ curation_history: PMID at NCBI. Source licensing responsibility was accepted by the maintainer; no cPSORTdb predictions or bulk prose were stored. llm_assisted: true +- timestamp: '2026-09-04T01:21:41Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a FUNCTION graph linking cortex-dependent core dehydration and multilayer + coat assembly to spore resistance. + llm_assisted: true +- timestamp: '2026-09-04T03:59:00Z' + curator: codex + action: ADD_CAUSAL_GRAPH + changes: Added a SpoIVA/CotE ASSEMBLY graph for Bacillus subtilis spore coat + morphogenesis, grounded cortex and coat nodes to their exact GO part terms, + and added primary evidence for SpoIVA-driven basement-layer assembly. + llm_assisted: true diff --git a/history/records/bacterial_type_flagellum/2026-09-04T014136Z-codex-b18360.yaml b/history/records/bacterial_type_flagellum/2026-09-04T014136Z-codex-b18360.yaml new file mode 100644 index 0000000..729edcf --- /dev/null +++ b/history/records/bacterial_type_flagellum/2026-09-04T014136Z-codex-b18360.yaml @@ -0,0 +1,22 @@ +history_version: 1 +target: + kind: record + path: data/structures/appendage/bacterial_type_flagellum.yaml + slug: bacterial_type_flagellum +session: + id: 2026-09-04T014136Z-codex-b18360 + timestamp: '2026-09-04T01:41:36Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Describe flagellum graph edges + details: Added descriptions to the remaining bacterial flagellum torque-generation graph + edges so the C-ring-to-rotor, motor-rotation-to-filament, and filament-to-swimming steps + are explicit while preserving the existing evidence. diff --git a/history/records/carboxysome/2026-09-04T014136Z-codex-d52ed9.yaml b/history/records/carboxysome/2026-09-04T014136Z-codex-d52ed9.yaml new file mode 100644 index 0000000..7af2163 --- /dev/null +++ b/history/records/carboxysome/2026-09-04T014136Z-codex-d52ed9.yaml @@ -0,0 +1,22 @@ +history_version: 1 +target: + kind: record + path: data/structures/microcompartment/carboxysome.yaml + slug: carboxysome +session: + id: 2026-09-04T014136Z-codex-d52ed9 + timestamp: '2026-09-04T01:41:36Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Describe carboxysome graph edges + details: Added descriptions to the remaining carboxysome CO2-concentrating and beta-carboxysome + assembly graph edges so shell pore transport, CO2 retention, RuBisCO fixation, cargo condensation, + shell-facet formation, and shell closure are explicit while preserving the existing evidence. diff --git a/history/records/cell_outer_membrane/2026-09-04T011019Z-codex-32cc8a.yaml b/history/records/cell_outer_membrane/2026-09-04T011019Z-codex-32cc8a.yaml new file mode 100644 index 0000000..e6d0aef --- /dev/null +++ b/history/records/cell_outer_membrane/2026-09-04T011019Z-codex-32cc8a.yaml @@ -0,0 +1,25 @@ +history_version: 1 +target: + kind: record + path: data/structures/envelope/cell_outer_membrane.yaml + slug: cell_outer_membrane +session: + id: 2026-09-04T011019Z-codex-32cc8a + timestamp: '2026-09-04T01:10:19Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add outer-membrane Lpt/BAM causal graph + details: Continued the causal-graph score ranking and curated the next rank-1 graphless + record, cell outer membrane. Added an ASSEMBLY graph for Lpt-mediated LPS transport to + the outer leaflet, BAM-mediated beta-barrel OMP assembly, and formation of the asymmetric + permeability barrier; the graph reuses the existing Silhavy, Kahne and Walker envelope + review and adds DOI-backed evidence for Lpt and BAM specificity. diff --git a/history/records/cell_outer_membrane/2026-09-04T040500Z-codex-f9c170.yaml b/history/records/cell_outer_membrane/2026-09-04T040500Z-codex-f9c170.yaml new file mode 100644 index 0000000..08d692d --- /dev/null +++ b/history/records/cell_outer_membrane/2026-09-04T040500Z-codex-f9c170.yaml @@ -0,0 +1,21 @@ +history_version: 1 +target: + kind: record + path: data/structures/envelope/cell_outer_membrane.yaml + slug: cell_outer_membrane +session: + id: 2026-09-04T040500Z-codex-f9c170 + timestamp: '2026-09-04T04:05:00Z' + actors: + - type: ai_agent + name: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Added an outer-membrane selective-permeability function graph + details: Added a FUNCTION causal graph for LPS and beta-barrel porin contributions to selective + outer-membrane permeability, grounded LPS nodes to CHEBI:16412, added Nikaido 2003 evidence + for hydrophobic exclusion and porin diffusion, and validated the edited CellStructureRecord + with linkml-validate. diff --git a/history/records/divisome_complex/2026-09-04T013928Z-codex-034eb4.yaml b/history/records/divisome_complex/2026-09-04T013928Z-codex-034eb4.yaml new file mode 100644 index 0000000..67092ea --- /dev/null +++ b/history/records/divisome_complex/2026-09-04T013928Z-codex-034eb4.yaml @@ -0,0 +1,23 @@ +history_version: 1 +target: + kind: record + path: data/structures/division_machinery/divisome_complex.yaml + slug: divisome_complex +session: + id: 2026-09-04T013928Z-codex-034eb4 + timestamp: '2026-09-04T01:39:28Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Expand divisome treadmilling graph + details: Continued the causal-graph score ranking from the poorest existing content gaps. + Expanded the divisome FUNCTION graph with an explicit FtsZ treadmilling process node and + evidence-backed edge descriptions for membrane tethering, Z-ring assembly, treadmilling + around the division site, synthase distribution, and septal peptidoglycan synthesis. diff --git a/history/records/encapsulin_nanocompartment/2026-09-04T011805Z-codex-da906f.yaml b/history/records/encapsulin_nanocompartment/2026-09-04T011805Z-codex-da906f.yaml new file mode 100644 index 0000000..47664f0 --- /dev/null +++ b/history/records/encapsulin_nanocompartment/2026-09-04T011805Z-codex-da906f.yaml @@ -0,0 +1,25 @@ +history_version: 1 +target: + kind: record + path: data/structures/microcompartment/encapsulin_nanocompartment.yaml + slug: encapsulin_nanocompartment +session: + id: 2026-09-04T011805Z-codex-da906f + timestamp: '2026-09-04T01:18:05Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add encapsulin cargo-loading iron-storage graph + details: Continued the causal-graph score ranking and curated the next rank-1 graphless + record, encapsulin nanocompartment. Added a FUNCTION graph linking HK97-fold shell self-assembly, + C-terminal targeting-peptide cargo loading, ferritin-like cargo encapsulation, Fe2+ mineralisation, + and iron/oxidative-stress buffering, reusing the existing encapsulin review evidence and + adding primary edge evidence from Sutter et al. 2008 and McHugh et al. 2014. diff --git a/history/records/encapsulin_nanocompartment/2026-09-04T042400Z-codex-0b3903.yaml b/history/records/encapsulin_nanocompartment/2026-09-04T042400Z-codex-0b3903.yaml new file mode 100644 index 0000000..8810aaa --- /dev/null +++ b/history/records/encapsulin_nanocompartment/2026-09-04T042400Z-codex-0b3903.yaml @@ -0,0 +1,21 @@ +history_version: 1 +target: + kind: record + path: data/structures/microcompartment/encapsulin_nanocompartment.yaml + slug: encapsulin_nanocompartment +session: + id: 2026-09-04T042400Z-codex-0b3903 + timestamp: '2026-09-04T04:24:00Z' + actors: + - type: ai_agent + name: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Added an encapsulin HK97 shell-assembly graph + details: Added an ASSEMBLY causal graph for HK97-fold encapsulin shell formation around + targeting-peptide-tagged cargo, anchored shell protein graph nodes with PF04454, grounded + the existing ferrous-iron node with CHEBI:29033, and validated the edited CellStructureRecord + with linkml-validate. diff --git a/history/records/endospore_external_encapsulating_structure/2026-09-04T012301Z-codex-eb0cc5.yaml b/history/records/endospore_external_encapsulating_structure/2026-09-04T012301Z-codex-eb0cc5.yaml new file mode 100644 index 0000000..3f42484 --- /dev/null +++ b/history/records/endospore_external_encapsulating_structure/2026-09-04T012301Z-codex-eb0cc5.yaml @@ -0,0 +1,23 @@ +history_version: 1 +target: + kind: record + path: data/structures/spore/endospore_external_encapsulating_structure.yaml + slug: endospore_external_encapsulating_structure +session: + id: 2026-09-04T012301Z-codex-eb0cc5 + timestamp: '2026-09-04T01:23:01Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Add endospore cortex and coat resistance graph + details: Continued the causal-graph score ranking and curated the final graphless record, + endospore external encapsulating structure. Added a FUNCTION graph linking cortex peptidoglycan + to core dehydration and heat resistance, and coat-protein assembly to the multilayered + enzyme and toxin barrier that protects dormant spores. diff --git a/history/records/endospore_external_encapsulating_structure/2026-09-04T034957Z-codex-d32d61.yaml b/history/records/endospore_external_encapsulating_structure/2026-09-04T034957Z-codex-d32d61.yaml new file mode 100644 index 0000000..4661385 --- /dev/null +++ b/history/records/endospore_external_encapsulating_structure/2026-09-04T034957Z-codex-d32d61.yaml @@ -0,0 +1,26 @@ +history_version: 1 +target: + kind: record + path: data/structures/spore/endospore_external_encapsulating_structure.yaml + slug: endospore_external_encapsulating_structure +session: + id: 2026-09-04T034957Z-codex-d32d61 + timestamp: '2026-09-04T03:49:57Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add endospore SpoIVA and CotE coat assembly graph + details: Continued the causal-graph score ranking after endospore external encapsulating + structure became the poorest record. Reviewed the existing cortex and coat resistance + graph, grounded cortex and endospore-coat structure nodes with their exact GO part terms, + and added a Bacillus subtilis ASSEMBLY graph that separates SpoIVA basement-layer self-assembly + and CotE-dependent outer-coat organization from the downstream resistance graph. Added + primary evidence for ATP-driven SpoIVA self-assembly and Driks et al. coat-protein localization. diff --git a/history/records/gas_vesicle/2026-09-04T011557Z-codex-73a905.yaml b/history/records/gas_vesicle/2026-09-04T011557Z-codex-73a905.yaml new file mode 100644 index 0000000..44aea7e --- /dev/null +++ b/history/records/gas_vesicle/2026-09-04T011557Z-codex-73a905.yaml @@ -0,0 +1,26 @@ +history_version: 1 +target: + kind: record + path: data/structures/inclusion/gas_vesicle.yaml + slug: gas_vesicle +session: + id: 2026-09-04T011557Z-codex-73a905 + timestamp: '2026-09-04T01:15:57Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add gas-vesicle GvpA/GvpC buoyancy graph + details: Continued the causal-graph score ranking and curated the next rank-1 graphless + record, gas vesicle. Added a FUNCTION graph linking GvpA shell polymerisation, ribbed + vesicle shell formation, GvpC-dependent strengthening, liquid-water exclusion by the gas-permeable + shell, and gas-filled buoyancy regulation, reusing the Walsby 1994 and Bayro et al. 2012 + evidence and using the existing Dutka et al. 2023 cryo-ET structural publication as additional + edge-level evidence. diff --git a/history/records/gas_vesicle/2026-09-04T041400Z-codex-c2ee88.yaml b/history/records/gas_vesicle/2026-09-04T041400Z-codex-c2ee88.yaml new file mode 100644 index 0000000..534da9e --- /dev/null +++ b/history/records/gas_vesicle/2026-09-04T041400Z-codex-c2ee88.yaml @@ -0,0 +1,21 @@ +history_version: 1 +target: + kind: record + path: data/structures/inclusion/gas_vesicle.yaml + slug: gas_vesicle +session: + id: 2026-09-04T041400Z-codex-c2ee88 + timestamp: '2026-09-04T04:14:00Z' + actors: + - type: ai_agent + name: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Added an accessory-Gvp gas-vesicle assembly graph + details: Added an ASSEMBLY causal graph that records accessory GvpF/GvpL-family interaction + evidence for recruiting GvpA-family shell proteins during gas-vesicle biogenesis, anchored + GvpA, GvpC, and GvpF/GvpL graph nodes with Pfam identifiers, and validated the edited + CellStructureRecord with linkml-validate. diff --git a/history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T011223Z-codex-b5961f.yaml b/history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T011223Z-codex-b5961f.yaml new file mode 100644 index 0000000..c9cd1f9 --- /dev/null +++ b/history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T011223Z-codex-b5961f.yaml @@ -0,0 +1,25 @@ +history_version: 1 +target: + kind: record + path: data/structures/envelope/gram_negative_bacterium_type_cell_wall.yaml + slug: gram_negative_bacterium_type_cell_wall +session: + id: 2026-09-04T011223Z-codex-b5961f + timestamp: '2026-09-04T01:12:23Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add Gram-negative wall tethering causal graph + details: Continued the causal-graph score ranking and curated the next rank-1 graphless + record, Gram-negative-bacterium-type cell wall. Added a FUNCTION graph for the thin periplasmic + peptidoglycan wall and outer-membrane lipoprotein links, bounded its mechanistic Lpp evidence + to canonical E. coli, and cited Mathelie-Guinlet and colleagues 2020 for peptidoglycan-outer + membrane coupling and envelope stiffness. diff --git a/history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T044300Z-codex-f64c03.yaml b/history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T044300Z-codex-f64c03.yaml new file mode 100644 index 0000000..ac366ad --- /dev/null +++ b/history/records/gram_negative_bacterium_type_cell_wall/2026-09-04T044300Z-codex-f64c03.yaml @@ -0,0 +1,21 @@ +history_version: 1 +target: + kind: record + path: data/structures/envelope/gram_negative_bacterium_type_cell_wall.yaml + slug: gram_negative_bacterium_type_cell_wall +session: + id: 2026-09-04T044300Z-codex-f64c03 + timestamp: '2026-09-04T04:43:00Z' + actors: + - type: ai_agent + name: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Added a Gram-negative Lpp tether-assembly graph + details: Added an ASSEMBLY causal graph for Braun lipoprotein maturation, Lol-pathway trafficking + to the outer membrane, and L,D-transpeptidase-mediated covalent attachment to the thin + peptidoglycan wall; anchored Lpp graph nodes with exact UniProt and Pfam identifiers; + and validated the edited CellStructureRecord with linkml-validate. diff --git a/history/records/magnetosome/2026-09-04T014136Z-codex-ea15e8.yaml b/history/records/magnetosome/2026-09-04T014136Z-codex-ea15e8.yaml new file mode 100644 index 0000000..3b6e510 --- /dev/null +++ b/history/records/magnetosome/2026-09-04T014136Z-codex-ea15e8.yaml @@ -0,0 +1,22 @@ +history_version: 1 +target: + kind: record + path: data/structures/membrane_organelle/magnetosome.yaml + slug: magnetosome +session: + id: 2026-09-04T014136Z-codex-ea15e8 + timestamp: '2026-09-04T01:41:36Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Describe magnetosome mineralisation edge + details: Added the missing description to the magnetosome chain-alignment graph edge that + converts imported iron into magnetite, preserving the existing Uebe and Schueler 2016 + evidence. diff --git a/history/records/methyl_accepting_chemotaxis_protein_complex/2026-09-04T043400Z-codex-99020e.yaml b/history/records/methyl_accepting_chemotaxis_protein_complex/2026-09-04T043400Z-codex-99020e.yaml new file mode 100644 index 0000000..3db76b6 --- /dev/null +++ b/history/records/methyl_accepting_chemotaxis_protein_complex/2026-09-04T043400Z-codex-99020e.yaml @@ -0,0 +1,23 @@ +history_version: 1 +target: + kind: record + path: data/structures/other/methyl_accepting_chemotaxis_protein_complex.yaml + slug: methyl_accepting_chemotaxis_protein_complex +session: + id: 2026-09-04T043400Z-codex-99020e + timestamp: '2026-09-04T04:34:00Z' + actors: + - type: ai_agent + name: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - discussions + summary: Added a chemoreceptor-array assembly graph and CheA-to-CheY edge + details: Added an ASSEMBLY causal graph for methyl-accepting chemotaxis protein trimers, + CheA/CheW core signaling units, and extended hexagonal array formation; anchored MCP and + CheW graph nodes with Pfam identifiers; added a Stewart 1997 CheA-to-CheY phosphotransfer + edge; resolved the phosphotransfer curation TODO; and validated the edited CellStructureRecord + with linkml-validate. diff --git a/history/records/mreb_filament/2026-09-04T010327Z-codex-4abcd4.yaml b/history/records/mreb_filament/2026-09-04T010327Z-codex-4abcd4.yaml new file mode 100644 index 0000000..5b1ea94 --- /dev/null +++ b/history/records/mreb_filament/2026-09-04T010327Z-codex-4abcd4.yaml @@ -0,0 +1,27 @@ +history_version: 1 +target: + kind: record + path: data/structures/cytoskeleton/mreb_filament.yaml + slug: mreb_filament +session: + id: 2026-09-04T010327Z-codex-4abcd4 + timestamp: '2026-09-04T01:03:27Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add MreB sidewall-synthesis causal graph + details: Continued from the causal-graph score ranking after type_iv_pilus and curated the + next rank-1 graphless record. Added a FUNCTION graph that links MreB polymerisation, RodZ + coupling, the separate elongasome record, GO:0009252 sidewall peptidoglycan synthesis, + and the existing METPO:1000681 rod-shaped trait. The graph reuses the reviewed MreB/shape + literature already on the record and the sidewall-synthesis review that grounds the elongasome + graph, while preserving the existing decision that the filament-to-machine relation is + not an xref equivalence. diff --git a/history/records/nucleoid/2026-09-04T011949Z-codex-9db5d8.yaml b/history/records/nucleoid/2026-09-04T011949Z-codex-9db5d8.yaml new file mode 100644 index 0000000..d3c2525 --- /dev/null +++ b/history/records/nucleoid/2026-09-04T011949Z-codex-9db5d8.yaml @@ -0,0 +1,26 @@ +history_version: 1 +target: + kind: record + path: data/structures/nucleoid/nucleoid.yaml + slug: nucleoid +session: + id: 2026-09-04T011949Z-codex-9db5d8 + timestamp: '2026-09-04T01:19:49Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add nucleoid NAP and supercoiling graph + details: Continued the causal-graph score ranking and curated the next rank-1 graphless + record, nucleoid. Added a FUNCTION graph linking chromosomal DNA, nucleoid-associated + protein binding, local DNA bending and bridging, negative-supercoil constraint, plectonemic + loop formation, and multiscale chromosome compaction into the nucleoid, reusing the existing + Dillon and Dorman 2010 evidence and adding Verma, Qian and Adhya 2019 for Escherichia + coli nucleoid architecture. diff --git a/history/records/peptidoglycan_based_cell_wall/2026-09-04T011330Z-codex-0fcf20.yaml b/history/records/peptidoglycan_based_cell_wall/2026-09-04T011330Z-codex-0fcf20.yaml new file mode 100644 index 0000000..9bdfb95 --- /dev/null +++ b/history/records/peptidoglycan_based_cell_wall/2026-09-04T011330Z-codex-0fcf20.yaml @@ -0,0 +1,26 @@ +history_version: 1 +target: + kind: record + path: data/structures/envelope/peptidoglycan_based_cell_wall.yaml + slug: peptidoglycan_based_cell_wall +session: + id: 2026-09-04T011330Z-codex-0fcf20 + timestamp: '2026-09-04T01:13:30Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add peptidoglycan Lipid II assembly graph + details: Continued the causal-graph score ranking and curated the next rank-1 graphless + record, peptidoglycan-based cell wall. Added an ASSEMBLY graph for glycosyltransferase + use of Lipid II precursors, glycan-strand polymerisation, DD-transpeptidase crosslinking, + and formation of the turgor-resistant murein sacculus, reusing the existing Vollmer, Blanot + and de Pedro 2008 evidence and adding Egan, Errington and Vollmer 2020 for peptidoglycan + synthesis regulation. diff --git a/history/records/peptidoglycan_based_cell_wall/2026-09-04T034706Z-codex-fc9767.yaml b/history/records/peptidoglycan_based_cell_wall/2026-09-04T034706Z-codex-fc9767.yaml new file mode 100644 index 0000000..bbdc5c3 --- /dev/null +++ b/history/records/peptidoglycan_based_cell_wall/2026-09-04T034706Z-codex-fc9767.yaml @@ -0,0 +1,27 @@ +history_version: 1 +target: + kind: record + path: data/structures/envelope/peptidoglycan_based_cell_wall.yaml + slug: peptidoglycan_based_cell_wall +session: + id: 2026-09-04T034706Z-codex-fc9767 + timestamp: '2026-09-04T03:47:06Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Ground peptidoglycan Lipid II assembly graph + details: Continued from the causal-graph score ranking after peptidoglycan-based cell wall + remained the poorest record. Reviewed the Lipid II assembly graph against primary literature, + added the MurJ flipping step that was missing between precursor synthesis and polymerisation, + grounded Lipid II to CHEBI:27692, anchored the MurJ, RodA/FtsW SEDS and penicillin-binding + transpeptidase nodes to Pfam or InterPro, and added primary evidence for MurJ flipping + plus RodA and FtsW peptidoglycan polymerase activity. Validated the edited YAML with linkml-validate + against CellStructureRecord before recording the change. diff --git a/history/records/proton_transporting_atp_synthase_complex/2026-09-04T014136Z-codex-90001a.yaml b/history/records/proton_transporting_atp_synthase_complex/2026-09-04T014136Z-codex-90001a.yaml new file mode 100644 index 0000000..332ddc8 --- /dev/null +++ b/history/records/proton_transporting_atp_synthase_complex/2026-09-04T014136Z-codex-90001a.yaml @@ -0,0 +1,23 @@ +history_version: 1 +target: + kind: record + path: data/structures/energy_complex/proton_transporting_atp_synthase_complex.yaml + slug: proton_transporting_atp_synthase_complex +session: + id: 2026-09-04T014136Z-codex-90001a + timestamp: '2026-09-04T01:41:36Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Describe ATP synthase graph edges + details: Added descriptions to the remaining ATP synthase rotary-catalysis graph edges so + proton flow through subunit a, c-ring and central-stalk rotation, catalytic-head cycling, + ATP formation, and participation in proton-motive-force-driven ATP synthesis are explicit + while preserving the existing evidence. diff --git a/history/records/ribosome/2026-09-04T014136Z-codex-3472a5.yaml b/history/records/ribosome/2026-09-04T014136Z-codex-3472a5.yaml new file mode 100644 index 0000000..90fc030 --- /dev/null +++ b/history/records/ribosome/2026-09-04T014136Z-codex-3472a5.yaml @@ -0,0 +1,22 @@ +history_version: 1 +target: + kind: record + path: data/structures/ribonucleoprotein/ribosome.yaml + slug: ribosome +session: + id: 2026-09-04T014136Z-codex-3472a5 + timestamp: '2026-09-04T01:41:36Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Describe ribosome graph edges + details: Added descriptions to the remaining ribosome elongation-cycle graph edges so the + aminoacyl-tRNA substrate role and EF-G-accelerated translocation within the ribosome are + explicit while preserving the existing evidence. diff --git a/history/records/s_layer/2026-09-04T013816Z-codex-b5801a.yaml b/history/records/s_layer/2026-09-04T013816Z-codex-b5801a.yaml new file mode 100644 index 0000000..11ea85f --- /dev/null +++ b/history/records/s_layer/2026-09-04T013816Z-codex-b5801a.yaml @@ -0,0 +1,23 @@ +history_version: 1 +target: + kind: record + path: data/structures/envelope/s_layer.yaml + slug: s_layer +session: + id: 2026-09-04T013816Z-codex-b5801a + timestamp: '2026-09-04T01:38:16Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Expand S-layer anchoring graph + details: Continued the causal-graph score ranking from the poorest existing graph after + the graphless records were curated. Expanded the S-layer ASSEMBLY graph from SLP self-assembly + alone to include SLH-domain carriage, secondary cell-wall polymer localization, SLH-SCWP + binding, and anchoring of the crystalline lattice on the Gram-positive envelope surface. diff --git a/history/records/type_iii_protein_secretion_system_complex/2026-09-04T012106Z-codex-02296d.yaml b/history/records/type_iii_protein_secretion_system_complex/2026-09-04T012106Z-codex-02296d.yaml new file mode 100644 index 0000000..60b29ac --- /dev/null +++ b/history/records/type_iii_protein_secretion_system_complex/2026-09-04T012106Z-codex-02296d.yaml @@ -0,0 +1,24 @@ +history_version: 1 +target: + kind: record + path: data/structures/secretion_system/type_iii_protein_secretion_system_complex.yaml + slug: type_iii_protein_secretion_system_complex +session: + id: 2026-09-04T012106Z-codex-02296d + timestamp: '2026-09-04T01:21:06Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + summary: Add type III secretion export graph + details: Continued the causal-graph score ranking and curated the next rank-1 graphless + record, type III protein secretion system complex. Added a FUNCTION graph linking inner-ring + basal-body organization, the outer-membrane secretin, the membrane export apparatus, the + helical needle filament, and the host-membrane translocon to unfolded effector secretion + through a continuous injectisome conduit. diff --git a/history/records/type_iv_pilus/2026-09-04T005809Z-codex-a42bf8.yaml b/history/records/type_iv_pilus/2026-09-04T005809Z-codex-a42bf8.yaml new file mode 100644 index 0000000..0fd3c7f --- /dev/null +++ b/history/records/type_iv_pilus/2026-09-04T005809Z-codex-a42bf8.yaml @@ -0,0 +1,26 @@ +history_version: 1 +target: + kind: record + path: data/structures/appendage/type_iv_pilus.yaml + slug: type_iv_pilus +session: + id: 2026-09-04T005809Z-codex-a42bf8 + timestamp: '2026-09-04T00:58:09Z' + actors: + - type: ai_agent + name: codex + model: gpt-5 + agent_tool: codex +events: +- type: EDIT + outcome: changed + sections: + - causal_graphs + - evidence + summary: Add type IV pilus extension-retraction graph + details: Ranked the corpus with scripts/score_causal_graphs.py, selected the rank-1 graphless + type IV pilus record, and added a FUNCTION causal graph for PilB-driven extension, pilin + polymerisation, distal surface attachment, PilT-driven retraction, and twitching motility. + The graph cites Hospenthal et al. 2017 for Gram-negative T4P biogenesis, Skerker and Berg + 2001 for direct extension/retraction observation, and Merz, So and Sheetz 2000 for PilT-dependent + force generation. Validated the edited record with linkml-validate and scripts/validate_strict.py. diff --git a/justfile b/justfile index 828e5d7..e122819 100644 --- a/justfile +++ b/justfile @@ -54,6 +54,10 @@ render-check: report *args: uv run python scripts/corpus_report.py {{args}} +# Rank records by causal-graph coverage and evidence quality, poorest first. +score-causal-graphs *args: + uv run python scripts/score_causal_graphs.py {{args}} + # Refresh the generated current-corpus block in README.md. docs-stats: uv run python scripts/check_docs.py --write diff --git a/pages/structures/appendage/bacterial_type_flagellum.html b/pages/structures/appendage/bacterial_type_flagellum.html index 354a8cf..f22f1b5 100644 --- a/pages/structures/appendage/bacterial_type_flagellum.html +++ b/pages/structures/appendage/bacterial_type_flagellum.html @@ -128,7 +128,7 @@

Evidence

Curation history

- +

Source: data/structures/appendage/bacterial_type_flagellum.yaml