flagellated
METPO:1000704 · CLASS · REVIEWED
A motile in which an organism possesses flagella for locomotion.
Flagellated locomotion mechanism
Edge evidence
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flagellar filament
confers
flagellated
METPO:2007700A flagellar filament is the locomotory appendage of flagellated cells.
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DOI:10.3390/biom9070279helical filamentous organelle responsible for motility
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flagellar hook
connects
flagellar filament
The hook couples the motor to the filament.
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DOI:10.3390/biom9070279hook as a universal joint
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flagellar basal body
rotates
flagellar filament
The basal body motor rotates the filament for propulsion.
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DOI:10.1016/S1937-6448(08)01402-0reversible rotary motor
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ion motive force
powers
flagellar stator complex
METPO:2007900Ion flux through stator complexes powers torque generation.
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DOI:10.3389/fmicb.2021.659464relationship between the IMF and the functioning
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chemotaxis signaling
regulates
flagellated
RO:0002211Chemotaxis signaling changes flagellar motor behavior and movement direction.
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DOI:10.3390/biom9070279regulate the direction of flagella-driven motility
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flagellar type III secretion system
exports
flagellar structural subunits
METPO:2007804The fT3SS exports flagellar structural subunits to the distal assembly site.
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DOI:10.1128/ecosalplus.esp-0011-2023
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FliH-FliI-FliJ ATPase complex
part of
flagellar type III secretion system
biolink:part_ofThe FliH-FliI-FliJ ATPase complex powers flagellar protein export by the fT3SS.
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DOI:10.1128/ecosalplus.esp-0011-2023
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FliD filament cap
enables
flagellar filament polymerization
RO:0002327The FliD filament cap aids polymerization of flagellin into the filament.
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DOI:10.3390/biom14121488
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FlgK/FlgL hook-filament junction
enables
flagellar filament polymerization
RO:0002327FlgK/FlgL hook-filament junction proteins are required for filament polymerization.
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DOI:10.3390/biom14121488
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flagellar filament polymerization
results in formation of
flagellar filament
Polymerization of flagellin subunits forms the flagellar filament.
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DOI:10.3390/biom14121488
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flagellar stator complex
has function
transmembrane H+ channel
RO:0000085The MotA-MotB stator complex acts as a transmembrane H+ channel powering rotation.
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DOI:10.3390/biom14121488
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CheY-P
regulates
flagellar rotational switching
RO:0002211CheY-P binding to the C ring causes flagellar rotational switching (CCW/CW).
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DOI:10.1038/s41564-024-01630-z
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flagellar rotational switching
regulates
flagellated
RO:0002211Switching of motor rotation direction modulates flagellated motility behavior.
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DOI:10.1128/ecosalplus.esp-0011-2023
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Provenance
- Source
- METPO (2025-11-25)
- Definition source
- DOI:10.3390/biom9070279
Parent traits (1)
Children (1)
Synonyms (1)
- flagella
kg-microbe context
Matched 1 kg-microbe node via direct_metpo.
METPO:1000704[-2.371, -2.707, -4.290, +4.186, …]
Nearest neighbors in embedding space
- morphology monotrichous 1.000
- morphology amphitrichous 1.000
- morphology lophotrichous 1.000
- morphology peritrichous 1.000
- morphology flagellar arrangement 1.000
- environment pH range mid2 0.443
- environment pH range mid1 0.437
- environment pH range mid3 0.433
Deep research
# 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
Curation history
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SEEDED_FROM_METPO · seed_from_metpo
imported from data/raw/metpo.owl (CLASS)
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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.
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GROUND_CAUSAL_PREDICATES · claude
Grounded 2 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002327×1, RO:0002211×1).
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RENAME_PREDICATE_LABELS · claude
Renamed 1 causal-edge predicate label(s) to align with existing groundings: powers → enables ×1.
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GROUND_CAUSAL_PREDICATES · claude
Grounded 1 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (RO:0002327×1).
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GROUND_CAUSAL_NODES · claude
Grounded 2 causal-node grounding field(s) via mappings/node_grounding.tsv (GO:0009420×1, GO:0009424×1).
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GROUND_CAUSAL_NODES · claude
Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (GO:0006935×1).
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ENRICH_CAUSAL_GRAPH · claude
Added 8 evidence-backed generic edges (9 new nodes) from the deep-research report.
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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).
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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.
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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.
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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.
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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.
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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.'