FvbA (PA4156) is a TonB-dependent outer-membrane receptor of Pseudomonas aeruginosa PAO1 required for the use of the Vibrio cholerae catecholate siderophore vibriobactin as an iron source. It is a close homologue of the V. cholerae vibriobactin receptor ViuA, with an N-terminal signal peptide, plug domain and TonB-dependent beta-barrel. Expression of fvbA is controlled by the iron regulator Fur, by vibriobactin and by the adjacent IclR-type regulator FvbR (PA4157).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0009279 cell outer membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Cell outer membrane from PAINT node PTN002824128, seeded by E. coli TonB-dependent receptors with direct localization (FepA P05825, BtuB P06129, CirA P17315 and YncD P76115). Reason: TonB-dependent receptors are 22-strand outer-membrane beta-barrels with an N-terminal plug; the family membership and the cleavable signal peptide agree with outer-membrane location. Supporting Evidence: file:PSEAE/PA4156/PA4156-uniprot.txt PF00593; TonB_dep_Rec_b-barrel file:PSEAE/PA4156/PA4156-uniprot.txt FT SIGNAL 1..29 |
| GO:0009279 cell outer membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Cell outer membrane from the UniProt subcellular location and family rule. Reason: Consistent with the IBA row; a TonB-dependent receptor barrel. Supporting Evidence: file:PSEAE/PA4156/PA4156-uniprot.txt PF00593; TonB_dep_Rec_b-barrel |
| GO:0015344 siderophore uptake transmembrane transporter activity | IBA GO_REF:0000033 | ACCEPT | Summary: Siderophore uptake transmembrane transporter activity from PAINT node PTN004738955 (PTHR30069 TonB-dependent siderophore receptor clade, 142 leaves in 21 taxa). Its four IBD seeds are the PAO1 receptors PfeA, ChtA (PA4675), FvbA (PA4156) and PirA, each through a PseudoCAP IMP row; the node is assessed in the PA4675 notes. Reason: Core function. The gene product is itself a seed of this IBD through an experimental row on its own ferric-siderophore uptake, which is expected, not circular; the node is grounded in four independently characterized PAO1 receptors and sits within a TonB-dependent siderophore receptor clade where ferric-siderophore uptake is the established function. Current UniProt places PA4156 in PANTHER PTHR32552 rather than PTHR30069; the IBA follows the PANTHER version used by PAINT, and the function is supported on this gene by its own mutant either way. Supporting Evidence: PMID:21546589 A P. aeruginosa mutant in the two endogenous siderophores (pyoverdine and pyochelin) and in fvbA was unable to utilize vibriobactin as an iron source. PMID:21546589 we identified a P. aeruginosa gene, PA4156 (fvbA), encoding a protein highly homologous to the V. cholerae vibriobactin receptor (ViuA) |
| GO:0015344 siderophore uptake transmembrane transporter activity | IMP PMID:21546589 FvbA is required for vibriobactin utilization in Pseudomonas... | ACCEPT | Summary: PseudoCAP IMP seed for the IBD at PTN004738955. A pyoverdine- and pyochelin-deficient strain also lacking fvbA cannot use vibriobactin as an iron source. Reason: Seed verdict SOUND. Loss of vibriobactin-dependent iron acquisition when the TonB-dependent receptor gene is inactivated, for a close homologue of the V. cholerae vibriobactin receptor ViuA, is direct genetic evidence that FvbA transports ferric vibriobactin across the outer membrane. Supporting Evidence: PMID:21546589 A P. aeruginosa mutant in the two endogenous siderophores (pyoverdine and pyochelin) and in fvbA was unable to utilize vibriobactin as an iron source. PMID:21546589 we identified a P. aeruginosa gene, PA4156 (fvbA), encoding a protein highly homologous to the V. cholerae vibriobactin receptor (ViuA) |
| GO:0015891 siderophore transport | IMP PMID:21546589 FvbA is required for vibriobactin utilization in Pseudomonas... | TOO GENERAL | Summary: PseudoCAP IMP; fvbA mutant cannot use vibriobactin. Reason: True but entailed by GO:0044718 siderophore transmembrane transport, accepted on this gene (is_a descendant). Supporting Evidence: PMID:21546589 A P. aeruginosa mutant in the two endogenous siderophores (pyoverdine and pyochelin) and in fvbA was unable to utilize vibriobactin as an iron source. |
| GO:0033214 siderophore-iron import into cell | IEA GO_REF:0000108 | ACCEPT | Summary: Siderophore-iron import into cell, inferred by GO from the molecular function row. Reason: The mutant phenotype is failure to acquire iron from vibriobactin, i.e. siderophore-mediated iron import. Supporting Evidence: PMID:21546589 A P. aeruginosa mutant in the two endogenous siderophores (pyoverdine and pyochelin) and in fvbA was unable to utilize vibriobactin as an iron source. |
| GO:0044718 siderophore transmembrane transport | IBA GO_REF:0000033 | ACCEPT | Summary: Siderophore transmembrane transport from PAINT node PTN004738955, seeded by E. coli CirA (P17315, IMP). Reason: Core process; TonB-dependent ferric-siderophore uptake across the outer membrane, shown for this receptor by its mutant phenotype. Supporting Evidence: PMID:21546589 A P. aeruginosa mutant in the two endogenous siderophores (pyoverdine and pyochelin) and in fvbA was unable to utilize vibriobactin as an iron source. |
| GO:0071281 cellular response to iron ion | EXP PMID:21546589 FvbA is required for vibriobactin utilization in Pseudomonas... | MARK AS OVER ANNOTATED | Summary: CollecTF annotation of the Fur target gene fvbA to cellular response to iron ion, from evidence that Fur regulates fvbA. Reason: The evidence is that fvbA expression is controlled by Fur (and by vibriobactin and FvbR), which makes the gene a Fur target, not a participant in the iron response; the abstract calls these analyses preliminary. Iron-regulated expression of a target gene is not by itself a role in responding to iron. Fur itself carries the response term. Supporting Evidence: PMID:21546589 preliminary analyses revealed the involvement of vibriobactin, Fur protein and an IclR-type regulator, FvbR (PA4157), in fvbA regulation |
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Download this section (compressed HTML)Experiment: Complement the fvbA mutant and measure radiolabelled ferric-vibriobactin uptake, and test vibriobactin binding by purified FvbA, to confirm the receptor-transporter role biochemically.
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