flagellated

METPO:1000704 · CLASS · REVIEWED

A motile in which an organism possesses flagella for locomotion.

Flagellated locomotion mechanism

Evidence-backed causal sketch linking the flagellated phenotype to flagellar filament, hook, basal body, stator, ion motive force, and chemotaxis.

Flagellated locomotion mechanism Interactive directed graph showing evidence-backed causal relationships for flagellated.

Edge evidence

  • flagellar filament confers flagellated METPO:2007700

    A flagellar filament is the locomotory appendage of flagellated cells.

    • DOI:10.3390/biom9070279 helical filamentous organelle responsible for motility Supports the filament as the locomotory flagellar structure.
  • flagellar hook connects flagellar filament

    The hook couples the motor to the filament.

    • DOI:10.3390/biom9070279 hook as a universal joint Supports the hook's coupling role.
  • flagellar basal body rotates flagellar filament

    The basal body motor rotates the filament for propulsion.

    • DOI:10.1016/S1937-6448(08)01402-0 reversible rotary motor Supports basal body motor rotation of flagella.
  • ion motive force powers flagellar stator complex METPO:2007900

    Ion flux through stator complexes powers torque generation.

    • DOI:10.3389/fmicb.2021.659464 relationship between the IMF and the functioning Supports ion motive force coupling to flagellar motor function.
  • chemotaxis signaling regulates flagellated RO:0002211

    Chemotaxis signaling changes flagellar motor behavior and movement direction.

    • DOI:10.3390/biom9070279 regulate the direction of flagella-driven motility Supports chemotaxis regulation of flagellated motility.
  • flagellar type III secretion system exports flagellar structural subunits METPO:2007804

    The fT3SS exports flagellar structural subunits to the distal assembly site.

    • DOI:10.1128/ecosalplus.esp-0011-2023 "a flagellar type III secretion system (fT3SS) at the base exports structural subunits from the cytoplasm through a narrow central channel to the distal tip where assembly occurs"
  • FliH-FliI-FliJ ATPase complex part of flagellar type III secretion system biolink:part_of

    The FliH-FliI-FliJ ATPase complex powers flagellar protein export by the fT3SS.

    • DOI:10.1128/ecosalplus.esp-0011-2023 "the ATPase ring complex (FliI, with FliH and FliJ) provides ATP hydrolysis for export"
  • FliD filament cap enables flagellar filament polymerization RO:0002327

    The FliD filament cap aids polymerization of flagellin into the filament.

    • DOI:10.3390/biom14121488 "flagellin subunits (~30,000) polymerize into a filament aided by a five-subunit FliD cap"
  • FlgK/FlgL hook-filament junction enables flagellar filament polymerization RO:0002327

    FlgK/FlgL hook-filament junction proteins are required for filament polymerization.

    • DOI:10.3390/biom14121488 "absence of FlgK/FlgL/FliD prevents filament polymerization"
  • flagellar filament polymerization results in formation of flagellar filament

    Polymerization of flagellin subunits forms the flagellar filament.

    • DOI:10.3390/biom14121488 "flagellin subunits (~30,000) polymerize into a filament" forming the helical filament.
  • flagellar stator complex has function transmembrane H+ channel RO:0000085

    The MotA-MotB stator complex acts as a transmembrane H+ channel powering rotation.

    • DOI:10.3390/biom14121488 "stator units formed by MotA and MotB ... act as a transmembrane H+ channel"
  • CheY-P regulates flagellar rotational switching RO:0002211

    CheY-P binding to the C ring causes flagellar rotational switching (CCW/CW).

    • DOI:10.1038/s41564-024-01630-z "Directional switching is triggered by the chemotaxis regulator CheY-P binding to FliM, causing full reversal of rotation"
  • flagellar rotational switching regulates flagellated RO:0002211

    Switching of motor rotation direction modulates flagellated motility behavior.

    • DOI:10.1128/ecosalplus.esp-0011-2023 "the C ring switches its conformational state" changing the direction of flagella-driven motility.

Provenance

Source
METPO (2025-11-25)
Definition source
DOI:10.3390/biom9070279

Parent traits (1)

Synonyms (1)

  • flagella RELATED_SYNONYM · metpo.owl

kg-microbe context

Matched 1 kg-microbe node via direct_metpo.

  • METPO:1000704 [-2.371, -2.707, -4.290, +4.186, …]

512-dim DeepWalkSkipGramEnsmallen embedding from kg-microbe (2026-04-25).

Nearest neighbors in embedding space

Top-8 cosine-similar METPO traits from the 2026-04-25 deepwalk (512-D).

Deep research

Generated by just research-trait; source: research/traits/morphology/flagellated-deep-research-falcon.md

Unreviewed literature output — not curated TraitMech content Ontology identifiers suggested below have not been resolved against their ontologies, and some are known to be wrong. Check any CURIE against the source before using it.
# Curation report: **flagellated**

## 1. Trait record and recommended scope

- **Trait label:** flagellated
- **Trait identifier:** **METPO:1000704**
- **Category / kind:** MORPHOLOGY / CLASS
- **Parent:** METPO:1000702
- **Reviewed definition supplied:** “A motile in which an organism possesses flagella for locomotion.”

For TraitMech, the operational phenotype should be **possession of at least one morphologically detectable locomotory flagellar appendage**, rather than active movement itself. A bacterial flagellum comprises a basal-body motor, hook, and helical filament; the filament is assembled from thousands of FliC/flagellin subunits and capped by FliD. The hook transmits motor torque to the filament, which acts as a propeller. (nedeljkovic2021bacterialflagellarfilament pages 1-2, minamino2023structureassemblyand pages 22-23)

### Scope boundaries

1. **Flagellated is not equivalent to motile.** A cell may possess an assembled but paralyzed flagellum because its stator, switch, ion motive force, or another motor component is defective. Conversely, surface translocation can be mediated by type-IV pili, surfactants, gliding systems, or growth and therefore does not establish flagellation. In *Pseudomonas aeruginosa*, PA4367 overexpression restored swarming in a Δ*fliA* background without restoring flagella by TEM and did not restore swimming, directly separating a surface-motility assay from flagellar morphology. (lo2016regulationofmotility pages 11-14)
2. **Swimming or soft-agar expansion is functional evidence, not sufficient morphological evidence.** The strongest phenotype annotation should use electron microscopy, flagellin-specific fluorescence, sheared-filament protein analysis, or another direct appendage assay. Motility assays should be represented as downstream observations.
3. **Swarming is compound and assay-specific.** It can require flagella but also surfactants, cell differentiation, surface hydration, and pili. It should not be used as a universal synonym for flagellation. (lo2016regulationofmotility pages 11-14)
4. **Archaella require a separate mechanistic branch.** Archaeal archaella are analogous locomotory appendages but are evolutionarily and mechanistically distinct from bacterial flagella: archaella assemble from the base and use ATP, whereas bacterial flagella assemble distally and use ion motive force for rotation. Whether METPO:1000704 intentionally includes archaella should be settled by ontology policy before adding archaeal mechanisms.
5. **Eukaryotic cilia/flagella are out of scope** for a bacterial flagellar graph. They are microtubule/dynein machines rather than homologues of bacterial flagella.
6. **Periplasmic flagella are included morphologically** if the intended taxonomic scope covers spirochetes, but they need a taxon-specific structural branch rather than assumptions copied from external flagella.

The supplied definition is therefore slightly circular (“A motile…”) and conflates structure with function. A curation-oriented wording would be: **“A microbial cell morphology in which the organism possesses one or more flagellar locomotory appendages.”** Add “whether or not actively rotating under the assay conditions” if METPO permits an editorial note.

## 2. Current mechanistic model

The best-supported bacterial causal chain is:

**flagellar transcriptional program → hook–basal-body assembly → assembly checkpoint and late-gene expression → flagellin export/polymerization → capped filament → ion-driven stator torque → hook-mediated torque transmission → filament rotation and propulsion.**

In the canonical *Salmonella/E. coli* hierarchy, FlhD/FlhC activates class-II genes needed for hook–basal-body construction. FlgM inhibits FliA/σ28 until hook–basal-body completion permits FlgM export; liberated FliA then drives class-III genes including *fliC*. This checkpoint couples morphological development to gene expression. (chilcott2000couplingofflagellar pages 7-8, chilcott2000couplingofflagellar pages 1-1, nedeljkovic2021bacterialflagellarfilament pages 9-10)

The flagellar type-III secretion system contains the membrane export gate FliP/Q/R–FlhA/B and cytoplasmic FliH/I/J complex. It transports structural subunits through the growing organelle. Recent synthesis describes FlhA docking of chaperone–substrate complexes—FlgN–FlgK/L, FliS–FliC, and FliT–FliD—and a FliK/FlhB-dependent switch from hook-type to filament-type export. The export gate can exploit electrochemical energy, with FlhA conducting H⁺ and Na⁺ under studied conditions. (minamino2023structureassemblyand pages 22-23)

FliC polymerization creates the helical filament, while FliD caps its distal end and supports elongation. Presence of the filament is the most direct molecular realization of the target morphology. (nedeljkovic2021bacterialflagellarfilament pages 1-2, nedeljkovic2021bacterialflagellarfilament pages 27-28)

For function, MotAB-family stators convert transmembrane ion flow into torque; many motors are H⁺-driven, whereas PomAB systems in taxa such as marine *Vibrio* are commonly Na⁺-driven. The hook acts as a universal joint, and the filament converts rotation into thrust. These are downstream causes of **flagellar motility**, but stator activity is not required for the narrow structural state “flagellated.” (nedeljkovic2021bacterialflagellarfilament pages 1-2, wu2024torquespeedrelationshipof pages 17-19, minamino2023structureassemblyand pages 22-23)

Chemotaxis regulates behavior rather than appendage presence. CheY-P binds the C-ring protein FliM and biases directional switching. Likewise, c-di-GMP-bound YcgR can alter motor direction and speed through a “backstop brake.” These edges belong downstream of the morphology node unless a taxon-specific pathway also regulates flagellar biogenesis. (mckee2013thesecondmessenger pages 10-11, nedeljkovic2021bacterialflagellarfilament pages 27-28)

## 3. Candidate nodes

### A. Trait and observed structures

- **flagellated:** `METPO:1000704`
- flagellar filament — candidate GO cellular-component grounding; verify the current GO release before YAML insertion
- bacterial-type flagellum — candidate GO cellular-component grounding; verify
- basal body; MS ring; C ring; rod; hook; hook–filament junction; filament cap
- polar flagellation, peritrichous flagellation, lateral flagellation, periplasmic flagellation — label-only phenotype candidates unless an approved morphology ontology term is found

### B. Transcriptional and assembly regulators

- FlhD/FlhC master regulator complex, preferably represented as **FlhD₄C₂** where supported
- FliA / σ28
- FlgM anti-σ28 factor
- FliK hook-length control/export-switch protein
- FlhB substrate-specificity switch component
- FleQ and alternative polar-flagellum regulators — **taxon-specific**, not substitutes for universal FlhDC

### C. Export and assembly machinery

Showing the first 60 of 236 lines of findings; the linked file also carries the run's front matter and the prompt it was given — read the full report.

Curation history

  1. · SEEDED_FROM_METPO · seed_from_metpo

    imported from data/raw/metpo.owl (CLASS)

  2. · CURATED_WITH_LITERATURE · codex

    Reviewed flagellated trait and added DOI-backed causal graph for flagellar filament, hook, basal body, stator, ion motive force, and chemotaxis.

  3. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 2 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002327×1, RO:0002211×1).

  4. · RENAME_PREDICATE_LABELS · claude

    Renamed 1 causal-edge predicate label(s) to align with existing groundings: powers → enables ×1.

  5. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 1 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002327×1).

  6. · GROUND_CAUSAL_NODES · claude

    Grounded 2 causal-node grounding field(s) via mappings/node_grounding.tsv (GO:0009420×1, GO:0009424×1).

  7. · GROUND_CAUSAL_NODES · claude

    Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (GO:0006935×1).

  8. · ENRICH_CAUSAL_GRAPH · claude

    Added 8 evidence-backed generic edges (9 new nodes) from the deep-research report.

  9. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 7 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002327×3, RO:0002211×2, METPO:2000209×1, RO:0000085×1).

  10. · MIGRATE_ENABLES_TRAIT_EDGES · claude

    Migrated 1 causal edge(s) off enables/RO:0002327 with a TRAIT object (1 to confers), issue 302. RO:0002327 has range 'biological process or activity', which a trait (a disposition) cannot satisfy, so the previous form entailed trait is-a BiologicalProcessOrActivity. The replacements are proposed in proposals/metpo_traitmech_v8 and are placeholder ids until METPO mints them.

  11. · MIGRATE_MICROBE_DOMAIN_EDGES_PART2 · claude

    Re-grounded 1 causal edge(s) off microbe-domain METPO predicates onto their causal-graph counterparts (1 to exports), issue 301 part 2. The previous predicates are transitively rdfs:subPropertyOf METPO:2000001, whose rdfs:domain is METPO:1000525 (microbe), so a causal-graph subject entailed that the subject IS a microbe; CausalNodeTypeEnum has no organism member, so no such edge could ever satisfy the domain. Each replacement is a 1:1 mirror of its source predicate that changes only the domain, so the claim each edge makes is unchanged and directions are unchanged. The replacements are proposed in proposals/metpo_traitmech_v9 and are placeholder ids until METPO mints them.

  12. · REGROUND_CAUSAL_EDGE · claude

    Re-grounded causal edge(s) off enables/RO:0002327 onto part of (biolink:part_of) and contributes to (RO:0002326), issue 334. biolink declares enables range 'biological process or activity', which only BIOLOGICAL_PROCESS, PATHWAY and MOLECULAR_FUNCTION satisfy, so an edge pointing at a GENE_OR_PROTEIN entailed a false type. The replacements are chosen per idiom rather than swept: a gene cluster ENCODES its product, a subunit is PART OF the complex it belongs to, and an energy source or acquired repertoire CONTRIBUTES TO the machine it powers or composes. All three declare no rdfs:domain or rdfs:range, so none can reintroduce the class of defect being removed.

  13. · REGROUND_CAUSAL_EDGE · claude

    Reverted the motive-force edge from contributes to back to enables/RO:0002327, issue 334 review. biolink defines contributes to as holding where one entity contributes to the occurrence or GENERATION of the other. A motive force does not generate the motor or machinery - it powers rotation, which is what the edge description says. That is the same energy-powers-a-machine idiom this work deferred for molecular_oxygen and cytoplasmic_na, so deferring it here too is the consistent call. The edge stays baselined under issue 334 until it is modelled as an input to the machine or pointed at the rotation process, either of which is range-correct.

  14. · REGROUND_CAUSAL_EDGE · claude

    Edge ion_motive_force -> stator_complex in graph flagellated_flagellar_motor: re-grounded it from enables/RO:0002327 to powers/METPO:2007900. Issue 334. biolink declares enables range 'biological process or activity', which of CausalNodeTypeEnum only BIOLOGICAL_PROCESS, PATHWAY and MOLECULAR_FUNCTION satisfy, so this edge entailed a false type on its object. 'Ion flux through stator complexes POWERS torque generation.'