FliP supplies the major repeated subunit of the FliPQR polypeptide channel and its gate, enabling axial subunits to cross the cytoplasmic membrane during flagellar construction. 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: fliP 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/fliP/fliP-uniprot.txt DR NCBIfam; TIGR01103; fliP; 1. |
| GO:0009306 protein secretion | IEA GO_REF:0000120 | MODIFY | Summary: fliP participates in flagellar type III protein export. 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. FliP supplies the major repeated subunit of the FliPQR polypeptide channel and its gate, enabling axial subunits to cross the cytoplasmic membrane during flagellar construction. GO:0030254 is an is_a/part_of descendant of the existing broad process; it identifies the actual transport mechanism. 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/fliP/fliP-uniprot.txt DR NCBIfam; TIGR01103; fliP; 1. |
| GO:0009425 bacterial-type flagellum basal body | IEA GO_REF:0000120 | MODIFY | Summary: fliP 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/fliP/fliP-uniprot.txt DR NCBIfam; TIGR01103; fliP; 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/fliP/fliP-uniprot.txt DR NCBIfam; TIGR01103; fliP; 1. |
| GO:0044781 bacterial-type flagellum organization | IEA GO_REF:0000104 | MODIFY | Summary: FliP contributes to building the flagellum through substrate export. 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. Assembly is the supported descendant of flagellum organization, with the FliPQR channel providing the actual protein-translocation route. Proposed replacements: bacterial-type flagellum assembly 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/fliP/fliP-uniprot.txt DR NCBIfam; TIGR01103; fliP; 1. |
Loading supporting content…
Download this section (compressed HTML)Q: Which ATPase/gate stoichiometry and ion-coupling conditions operate in native KT2440, and how strongly do export bypass phenotypes transfer from Salmonella?
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)