FliR supplies a distinct structural subunit of the FliPQR polypeptide channel, participating in gating and the interface with the proximal flagellar rod. In Pseudomonas putida KT2440 these functions are inferred from its conserved flagellar export-family identity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: fliR acts at the cytoplasmic-membrane export apparatus. Reason: The KT2440 assignment is inferred from the target-specific NCBIfam/InterPro classification and conserved export-system context; the mechanistic experiments cited here used Salmonella, not KT2440. The gate acts across the plasma membrane. Its assembly and detailed topology are distinguished from a generic membrane prediction. Primary cryo-EM shows noncanonical membrane topology, so this localization does not claim that each isolated subunit retains a conventional transmembrane-helix arrangement in the assembled channel. Supporting Evidence: PMID:29967543 The complex is a P5Q4R1 assembly consistent with the dominant species in our earlier nMS data of the flagellar system PMID:39766194 FliP and FliR assemble into the FliP5-FliR1 complex, and 4 FliQ subunits then bind to the FliP5-FliR1 complex to form the FliP5-FliQ4-FliR1 complex that allows proteins of the axial structure of the flagellum to pass through the cytoplasmic membrane file:PSEPK/fliR/fliR-uniprot.txt DR NCBIfam; TIGR01400; fliR; 1. |
| GO:0006605 protein targeting | IEA GO_REF:0000120 | MODIFY | Summary: FliR conducts substrates as a channel subunit rather than being a demonstrated targeting-signal receptor. Reason: The KT2440 assignment is inferred from the target-specific NCBIfam/InterPro classification and conserved export-system context; the mechanistic experiments cited here used Salmonella, not KT2440. The supported work is translocation through the FliPQR channel. Replace the targeting claim with the type III secretion process as an explicit lateral correction, not a claimed ontology descendant relationship. Proposed replacements: protein secretion by the type III secretion system Supporting Evidence: PMID:29967543 The complex is a P5Q4R1 assembly consistent with the dominant species in our earlier nMS data of the flagellar system PMID:39766194 FliP and FliR assemble into the FliP5-FliR1 complex, and 4 FliQ subunits then bind to the FliP5-FliR1 complex to form the FliP5-FliQ4-FliR1 complex that allows proteins of the axial structure of the flagellum to pass through the cytoplasmic membrane file:PSEPK/fliR/fliR-uniprot.txt DR NCBIfam; TIGR01400; fliR; 1. |
| GO:0009425 bacterial-type flagellum basal body | IEA GO_REF:0000120 | MODIFY | Summary: fliR belongs to the export apparatus at the base of the flagellum. Reason: The KT2440 assignment is inferred from the target-specific NCBIfam/InterPro classification and conserved export-system context; the mechanistic experiments cited here used Salmonella, not KT2440. GO:0120102 is a part_of descendant of the flagellum basal body and flagellum terms and identifies the protein export machinery precisely. Proposed replacements: bacterial-type flagellum secretion apparatus Supporting Evidence: PMID:29967543 The complex is a P5Q4R1 assembly consistent with the dominant species in our earlier nMS data of the flagellar system PMID:29946050 The flagellar protein export apparatus consists of the transmembrane gate complex formed by FlhA, FlhB, FliP, FliQ, and FliR and the cytoplasmic ATPase complex composed of FliH, FliI, and FliJ file:PSEPK/fliR/fliR-uniprot.txt DR NCBIfam; TIGR01400; fliR; 1. |
| GO:0016020 membrane | IEA GO_REF:0000120 | MODIFY | Summary: The membrane association is correctly localized more specifically to the plasma membrane. Reason: The KT2440 assignment is inferred from the target-specific NCBIfam/InterPro classification and conserved export-system context; the mechanistic experiments cited here used Salmonella, not KT2440. GO:0005886 is an is_a descendant of GO:0016020 and is already present. This is a specificity correction, not a reason to mark true membrane localization non-core. Proposed replacements: plasma membrane Supporting Evidence: PMID:29967543 The complex is a P5Q4R1 assembly consistent with the dominant species in our earlier nMS data of the flagellar system PMID:39766194 FliP and FliR assemble into the FliP5-FliR1 complex, and 4 FliQ subunits then bind to the FliP5-FliR1 complex to form the FliP5-FliQ4-FliR1 complex that allows proteins of the axial structure of the flagellum to pass through the cytoplasmic membrane file:PSEPK/fliR/fliR-uniprot.txt DR NCBIfam; TIGR01400; fliR; 1. |
| GO:0044780 bacterial-type flagellum assembly | IEA GO_REF:0000120 | ACCEPT | Summary: fliR performs a component step of flagellar construction. Reason: The KT2440 assignment is inferred from the target-specific NCBIfam/InterPro classification and conserved export-system context; the mechanistic experiments cited here used Salmonella, not KT2440. FliR supplies a distinct structural subunit of the FliPQR polypeptide channel, participating in gating and the interface with the proximal flagellar rod. This is direct machinery participation: it exports or guides structural substrates, rather than merely being required in a knockout experiment. Supporting Evidence: PMID:29967543 The complex is a P5Q4R1 assembly consistent with the dominant species in our earlier nMS data of the flagellar system PMID:39766194 FliP and FliR assemble into the FliP5-FliR1 complex, and 4 FliQ subunits then bind to the FliP5-FliR1 complex to form the FliP5-FliQ4-FliR1 complex that allows proteins of the axial structure of the flagellum to pass through the cytoplasmic membrane file:PSEPK/fliR/fliR-uniprot.txt DR NCBIfam; TIGR01400; fliR; 1. |
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