PvdT (PA2390) is the inner-membrane ATP-binding/permease component of the tripartite PvdRT-OpmQ efflux pump of Pseudomonas aeruginosa, a MacB-type ABC exporter together with the periplasmic membrane fusion protein PvdR and the TolC-like outer-membrane channel OpmQ. The pump takes up the siderophore pyoverdine on the periplasmic side and moves it to the extracellular medium. It secretes newly synthesized pyoverdine after the final maturation steps in the periplasm, recycles pyoverdine released after ferri-pyoverdine uptake through FpvA, and expels pyoverdine complexed with unwanted metals. Mutants lacking any component accumulate pyoverdine in the periplasm. The operon is iron-regulated under the pyoverdine sigma factor PvdS. The pump does not contribute to antibiotic resistance.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002049 pyoverdine biosynthetic process | IMP PMID:12686626 Identification and characterization of novel pyoverdine synt... | REMOVE | Summary: PseudoCAP IMP pyoverdine biosynthetic process from a mutant screen scored by pyoverdine production. PvdT is the exporter of the finished siderophore: mutants still make pyoverdine but trap it in the periplasm. Reason: Indirect phenotype. Reduced extracellular pyoverdine in a pvdT mutant reflects failed export from the periplasm, not a step of the biosynthesis. The process PvdT takes part in is siderophore transmembrane transport, proposed as a NEW row. Supporting Evidence: PMID:12686626 The candidate genes were mutated and the effects of the mutations on pyoverdine production were determined PMID:19906986 nearly all intracellular PVD was associated with the periplasmic fraction of pvdR , pvdT , and opmQ mutants PMID:21035449 Bacteria lacking this efflux pump accumulated PVD, or a fluorescent precursor, in the periplasm, due to their inability to efficiently secrete into the media newly synthesized PVD |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO ATP binding from the ABC ATPase domain. Reason: PvdT has an N-terminal ABC ATPase domain that energizes the pump. Supporting Evidence: file:PSEAE/pvdT/pvdT-uniprot.txt PF00005; ABC_tran PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: IBA plasma membrane from PTN001254814, seeded by E. coli MacB and B. subtilis O31712. Reason: Four predicted transmembrane helices in a MacB/FtsX permease domain; inner membrane location. Supporting Evidence: file:PSEAE/pvdT/pvdT-uniprot.txt Cell inner membrane file:PSEAE/pvdT/pvdT-uniprot.txt PF02687; FtsX PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location mapping (cell inner membrane). Reason: Same claim as the IBA row; consistent with the topology. Supporting Evidence: file:PSEAE/pvdT/pvdT-uniprot.txt Cell inner membrane PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. |
| GO:0015562 efflux transmembrane transporter activity | IDA PMID:19906986 Molecular basis of pyoverdine siderophore recycling in Pseud... | ACCEPT | Summary: PseudoCAP IDA (fluorescence and fractionation of mutants); one of the rows seeding PTN001254814. Reason: Core activity. PvdT is the inner-membrane ABC (MacB-type) component of the PvdRT-OpmQ pump, and loss of any component traps pyoverdine in the periplasm; efflux transmembrane transporter activity is the right level for the energizing subunit of a tripartite exporter. Supporting Evidence: PMID:19906986 we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0015562 efflux transmembrane transporter activity | IDA PMID:21035449 An efflux pump is involved in secretion of newly synthesized... | ACCEPT | Summary: PseudoCAP IDA; secretion of newly synthesized pyoverdine. Reason: Core activity. PvdT is the inner-membrane ABC (MacB-type) component of the PvdRT-OpmQ pump, and loss of any component traps pyoverdine in the periplasm; efflux transmembrane transporter activity is the right level for the energizing subunit of a tripartite exporter. Supporting Evidence: PMID:19906986 we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0015562 efflux transmembrane transporter activity | IDA PMID:22187978 The PvdRT-OpmQ efflux pump controls the metal selectivity of... | ACCEPT | Summary: PseudoCAP IDA; export of pyoverdine-metal complexes. Reason: Core activity. PvdT is the inner-membrane ABC (MacB-type) component of the PvdRT-OpmQ pump, and loss of any component traps pyoverdine in the periplasm; efflux transmembrane transporter activity is the right level for the energizing subunit of a tripartite exporter. Supporting Evidence: PMID:19906986 we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0015562 efflux transmembrane transporter activity | IMP PMID:19906986 Molecular basis of pyoverdine siderophore recycling in Pseud... | ACCEPT | Summary: PseudoCAP IMP; periplasmic accumulation in pvdT mutants. Reason: Core activity. PvdT is the inner-membrane ABC (MacB-type) component of the PvdRT-OpmQ pump, and loss of any component traps pyoverdine in the periplasm; efflux transmembrane transporter activity is the right level for the energizing subunit of a tripartite exporter. Supporting Evidence: PMID:19906986 we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0015562 efflux transmembrane transporter activity | IMP PMID:22187978 The PvdRT-OpmQ efflux pump controls the metal selectivity of... | ACCEPT | Summary: PseudoCAP IMP; metal-complex accumulation in pump mutants. Reason: Core activity. PvdT is the inner-membrane ABC (MacB-type) component of the PvdRT-OpmQ pump, and loss of any component traps pyoverdine in the periplasm; efflux transmembrane transporter activity is the right level for the energizing subunit of a tripartite exporter. Supporting Evidence: PMID:19906986 we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0015562 efflux transmembrane transporter activity | IMP PMID:23766114 An efflux pump is required for siderophore recycling by Pseu... | ACCEPT | Summary: PseudoCAP IMP; failed pyoverdine recycling in pump mutants. Reason: Core activity. PvdT is the inner-membrane ABC (MacB-type) component of the PvdRT-OpmQ pump, and loss of any component traps pyoverdine in the periplasm; efflux transmembrane transporter activity is the right level for the energizing subunit of a tripartite exporter. Supporting Evidence: PMID:19906986 we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0016020 membrane | IEA GO_REF:0000120 | TOO GENERAL | Summary: ARBA/InterPro membrane. Reason: True, but entailed by the accepted plasma membrane rows. Supporting Evidence: file:PSEAE/pvdT/pvdT-uniprot.txt Cell inner membrane |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO ATP hydrolysis activity. Reason: The ABC domain hydrolyses ATP to drive export, as for MacB; part of the energizing mechanism. Supporting Evidence: file:PSEAE/pvdT/pvdT-uniprot.txt PF00005; ABC_tran PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0022857 transmembrane transporter activity | IBA GO_REF:0000033 | TOO GENERAL | Summary: IBA from PTN001254814 (MacB-like clade, 118 leaves in 36 taxa), seeded by E. coli MacB P75831 and PvdT itself. Reason: True, but entailed by the accepted GO:0015562 efflux transmembrane transporter activity rows (is_a GO:0022857). The broad node term suits a MacB-type clade whose members export different substrates, and the IBD stands on MacB. Supporting Evidence: PMID:19906986 we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0055085 transmembrane transport | IEA GO_REF:0000120 | TOO GENERAL | Summary: IEA transmembrane transport inferred from the MF rows. Reason: True, but entailed by the proposed GO:0044718 siderophore transmembrane transport. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. |
| GO:1990281 efflux pump complex | IDA PMID:19906986 Molecular basis of pyoverdine siderophore recycling in Pseud... | ACCEPT | Summary: PseudoCAP IDA efflux pump complex. Reason: PvdT is the inner-membrane component of the tripartite PvdRT-OpmQ efflux pump. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:1990281 efflux pump complex | IDA PMID:21035449 An efflux pump is involved in secretion of newly synthesized... | ACCEPT | Summary: PseudoCAP IDA efflux pump complex. Reason: PvdT is the inner-membrane component of the tripartite PvdRT-OpmQ efflux pump. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:1990281 efflux pump complex | IDA PMID:22187978 The PvdRT-OpmQ efflux pump controls the metal selectivity of... | ACCEPT | Summary: PseudoCAP IDA efflux pump complex. Reason: PvdT is the inner-membrane component of the tripartite PvdRT-OpmQ efflux pump. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:1990281 efflux pump complex | IMP PMID:19906986 Molecular basis of pyoverdine siderophore recycling in Pseud... | ACCEPT | Summary: PseudoCAP IMP efflux pump complex. Reason: PvdT is the inner-membrane component of the tripartite PvdRT-OpmQ efflux pump. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:1990281 efflux pump complex | IMP PMID:22187978 The PvdRT-OpmQ efflux pump controls the metal selectivity of... | ACCEPT | Summary: PseudoCAP IMP efflux pump complex. Reason: PvdT is the inner-membrane component of the tripartite PvdRT-OpmQ efflux pump. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:1990281 efflux pump complex | IMP PMID:23766114 An efflux pump is required for siderophore recycling by Pseu... | ACCEPT | Summary: PseudoCAP IMP efflux pump complex. Reason: PvdT is the inner-membrane component of the tripartite PvdRT-OpmQ efflux pump. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 PvdRT-OpmQ displays the typical architecture of Gram-negative tripartite ABC-type exporters, consisting of an IM component with both ATPase and permease domains, a periplasmic membrane fusion protein, and a TolC-like OM protein |
| GO:0044718 siderophore transmembrane transport | IMP PMID:19906986 Molecular basis of pyoverdine siderophore recycling in Pseud... | NEW | Summary: Proposed process. PvdT, with PvdR and OpmQ, moves pyoverdine from the periplasm to the extracellular medium, for newly made, recycled and metal-loaded siderophore. Reason: PvdT does the work: it is the energizing inner-membrane component of the exporter. Replaces the removed pyoverdine biosynthetic process row as the correct process. Supporting Evidence: PMID:19906986 Therefore, the entire PvdRT-OpmQ system (i.e., the IM ABC transporter PvdT, the periplasmic fusion protein PvdR, and the OM porin OpmQ) appears to be involved in the transport of PVD from the periplasm to the extracellular milieu. PMID:19906986 nearly all intracellular PVD was associated with the periplasmic fraction of pvdR , pvdT , and opmQ mutants PMID:21035449 Bacteria lacking this efflux pump accumulated PVD, or a fluorescent precursor, in the periplasm, due to their inability to efficiently secrete into the media newly synthesized PVD PMID:23766114 Mutation of genes encoding this efflux pump (named PvdRT-OpmQ) prevented recycling of PVDI from the periplasm into the extracellular medium |
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