pvdT encodes the ATP-binding/permease component of the PvdRT-OpmQ tripartite pyoverdine export system. PvdT is an inner-membrane ABC transporter component that binds pyoverdine and hydrolyzes ATP to drive secretion and recycling of the siderophore pyoverdine, supporting iron acquisition under iron-limited conditions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: ATP binding is required for the ABC transporter ATPase, but ATP hydrolysis is the more informative function. Reason: Retain as non-core nucleotide binding. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt KM=0.164 mM for ATP |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: PvdT is an inner/cell membrane multi-pass transporter component; GOA uses plasma membrane for bacterial cell membrane. Reason: Retain the location annotation. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt SUBCELLULAR LOCATION: Cell inner membrane file:PSEPK/pvdT/pvdT-deep-research-falcon.md Inner membrane (as the ABC ATPase/TMD component of the tripartite system spanning inner membrane |
| GO:0016020 membrane | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Generic membrane is less informative than the retained plasma/cell membrane annotation. Reason: Retain GO:0005886 instead. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt SUBCELLULAR LOCATION: Cell inner membrane |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: ATP hydrolysis is the directly assayed energy-coupling activity of PvdT. Purified PvdT was shown biochemically to possess ATPase activity (PMID:36807028), and falcon deep research confirms PvdT is the ATP-hydrolyzing inner-membrane component of the PvdRT-OpmQ exporter. Reason: Retain as a core molecular-function annotation directly supported by biochemical assay of purified PvdT. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt This subunit binds PVD and drives file:PSEPK/pvdT/pvdT-uniprot.txt its secretion by hydrolyzing ATP PMID:36807028 We show that PvdT possesses an ATPase activity that is stimulated by the addition of PvdR file:PSEPK/pvdT/pvdT-deep-research-falcon.md PvdT is an ATP-hydrolyzing component consistent with an ABC exporter |
| GO:0022857 transmembrane transporter activity | IEA GO_REF:0000120 | ACCEPT | Summary: PvdT is the ATP-binding/permease component of a pyoverdine export system, so transporter activity is supported. Reason: Retain until a pyoverdine-specific transporter GO term is available in the review. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt Part of the tripartite efflux system PvdRT-OpmQ required for file:PSEPK/pvdT/pvdT-uniprot.txt the secretion into the extracellular milieu of the siderophore file:PSEPK/pvdT/pvdT-deep-research-falcon.md pyoverdine as the relevant substrate/ligand for the PvdT-containing complex |
| GO:0042626 ATPase-coupled transmembrane transporter activity | IC PMID:36807028 The ABC transporter family efflux pump PvdRT-OpmQ of Pseudom... | NEW | Summary: PvdT is the ATPase/permease component of the PvdRT-OpmQ export system and contributes to ATPase-coupled pyoverdine transport. Reason: This term is more specific than generic transmembrane transporter activity while avoiding the overclaim that PvdT alone performs the full tripartite export reaction. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt This subunit binds PVD and drives PMID:36807028 PvdT possesses an ATPase activity that is stimulated by the addition of PvdR file:PSEPK/pvdT/pvdT-deep-research-falcon.md PvdT is the inner-membrane ABC (MacB-like) ATPase/permease component file:PSEPK/pvdT/pvdT-deep-research-falcon.md energizes export by ATP hydrolysis and forms a functional complex with the periplasmic adaptor |
| GO:0055085 transmembrane transport | IEA GO_REF:0000108 | ACCEPT | Summary: PvdT participates directly in transmembrane export of pyoverdine. Genetic disruption of pvdRT-opmQ reduces pyoverdine in the medium (PMID:30346656), and falcon deep research frames the system as mediating secretion of newly synthesized and recycled pyoverdine. Reason: Retain the process annotation. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt responsible for export of newly synthesized PVD after the final steps PMID:30346656 Deletion of pvdRT-opmQ leads to reduced amounts of pyoverdine in the medium and decreased growth under iron limitation file:PSEPK/pvdT/pvdT-deep-research-falcon.md secretion of newly synthesized and recycled pyoverdine |
| GO:1902495 transmembrane transporter complex | IEA GO_REF:0000117 | ACCEPT | Summary: PvdT is part of the tripartite PvdRT-OpmQ transporter complex, working with the periplasmic adaptor PvdR and outer-membrane channel OpmQ. Reason: Retain the complex annotation. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt composed of an inner membrane component with both ATPase and permease file:PSEPK/pvdT/pvdT-deep-research-falcon.md energizes export by ATP hydrolysis and forms a functional complex with the periplasmic adaptor |
| GO:0005886 plasma membrane | EXP PMID:36807028 The ABC transporter family efflux pump PvdRT-OpmQ of Pseudom... | ACCEPT | Summary: PvdT is an inner/cell membrane multi-pass transporter component; GOA uses plasma membrane for bacterial cell membrane. Inner-membrane localization was directly determined for purified PvdT (PMID:36807028). Reason: Retain the location annotation; experimentally supported subcellular localization. Supporting Evidence: file:PSEPK/pvdT/pvdT-uniprot.txt SUBCELLULAR LOCATION: Cell inner membrane |
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Download this section (compressed HTML)Q: Does PvdT directly determine pyoverdine substrate specificity, or is substrate recognition mainly imposed by PvdR/OpmQ or other pyoverdine pathway components?
Suggested experts: Pseudomonas siderophore transport experts
Experiment: Reconstitute PvdRT-OpmQ variants with ATPase-dead PvdT and PvdR-interaction mutants, then measure pyoverdine binding, ATP hydrolysis, and export in iron-limited cells or proteoliposomes.
Type: transporter reconstitution and secretion assay
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