FliC is the b-type flagellin of Pseudomonas aeruginosa PAO1, the subunit that polymerises to form the filament of the single polar flagellum. Flagellin is exported through the flagellar type III export apparatus, travels through the hollow filament and is assembled at the distal tip beneath the FliD cap. The filament acts as the propeller of flagellum-dependent swimming motility, and loss of fliC abolishes motility. Flagellin is also a major surface antigen and a ligand recognised by host innate immunity, and fliC mutants are attenuated in mouse models of acute lung infection. P. aeruginosa strains carry either an a-type (as in strain PAK) or a b-type (as in PAO1) flagellin.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0071973 bacterial-type flagellum-dependent cell motility | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PTN001250065, seeded by PAO1 FliC itself and H. pylori FlaA (P0A0S1, IMP swarming motility, a descendant term). Reason: Flagellin forms the filament, the propeller of flagellar motility, so it does part of the work of the process. The IBD stands on the H. pylori seed even with the PseudoCAP row downgraded to a mutant phenotype, and the term suits a flagellin clade. Supporting Evidence: file:PSEAE/fliC/fliC-uniprot.txt Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. PMID:9423837 Nonmotile mutants of PAK were analyzed to confirm that the expected gene replacement events, in which the interrupted copy of fliC , the gene encoding flagellin protein, introduced into PAK and PAK/NP had replaced the wild-type coding sequence, had occurred. |
| GO:0005198 structural molecule activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO mapping of the flagellin domains. Flagellin is the structural subunit of the flagellar filament. Reason: Structural constituent of the filament is the molecular role of flagellin; this matches the structural-molecule core function used for the FliD cap in this review set. Supporting Evidence: file:PSEAE/fliC/fliC-uniprot.txt Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Mapping of the UniProt Secreted location. Flagellin is exported and assembles outside the cell envelope, and free flagellin is also released. Reason: True, but the filament term says where flagellin acts and is not a descendant of extracellular region, so this row cannot be refined; kept as a peripheral location, as for FliD. Supporting Evidence: file:PSEAE/fliC/fliC-uniprot.txt SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. |
| GO:0009288 bacterial-type flagellum | IEA GO_REF:0000120 | MODIFY | Summary: Correct but general: flagellin is the subunit of the flagellar filament. Reason: GO:0009420 bacterial-type flagellum filament is part_of GO:0009288 and is the compartment flagellin builds, so the specific term should replace the general one, as done for FliD with the filament cap term. This is not a root organelle term. Proposed replacements: bacterial-type flagellum filament Supporting Evidence: file:PSEAE/fliC/fliC-uniprot.txt Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. |
| GO:0071973 bacterial-type flagellum-dependent cell motility | IDA PMID:9423837 Role of flagella in pathogenesis of Pseudomonas aeruginosa p... | ACCEPT | Summary: PseudoCAP row and a seed of PTN001250065. The paper shows that fliC disruption mutants of strain PAK are nonmotile; it reports no direct assay of flagellin in motility. Reason: The process is right for flagellin. The evidence is a mutant phenotype (IMP, not IDA), obtained on the a-type fliC of strain PAK rather than the PAO1 b-type allele annotated here; both are orthologous flagellin genes of the same species, so the claim transfers, and the defect is the evidence code. Supporting Evidence: PMID:9423837 Nonmotile mutants of PAK were analyzed to confirm that the expected gene replacement events, in which the interrupted copy of fliC , the gene encoding flagellin protein, introduced into PAK and PAK/NP had replaced the wild-type coding sequence, had occurred. |
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Download this section (compressed HTML)Q: Does the b-type flagellin of PAO1 differ from the a-type flagellin of PAK in filament assembly or motility performance, beyond its antigenic and glycosylation differences?
Experiment: Swimming and swarming assays of a clean PAO1 fliC deletion complemented with the PAO1 b-type or the PAK a-type fliC allele.
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