Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
UniProtKB record A0A0H2M6I3 (A0A0H2M6I3_VARPD) - Phosphate transport system permease protein PstA from Variovorax paradoxus TBEA6
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VPARA_10460 (pstA, A0A0H2M6I3) is a 294-aa six-pass inner-membrane ABC permease subunit (InterPro IPR005672, NCBIfam TIGR00974, NCBIfam NF008430, PANTHER PTHR42922:SF1, PROSITE PS50928) encoded on contig JZWI01000005 (KLN58034.1).
"CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU363043}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363043}."
Arg-220 of the PstA protein is required for phosphate transport through the phosphate-specific transport system in Escherichia coli but not for alkaline phosphatase repression.
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Site-directed substitution of Arg220 in E. coli PstA (corresponding to Arg220 in VPARA_10460) abolishes phosphate transport through the Pst system while preserving alkaline phosphatase repression.
"The Arg-220----Gln mutation resulted in the loss of phosphate transport through the phosphate-specific transport system, but the alkaline phosphatase activity remained repressed."
Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships.
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Establishes the sequence and organization of pstA within the phoS-pstC-pstA-pstB-phoU operon.
"The complete sequence is transcribed counterclockwise, in the order phoS pstC pstA pstB phoU."
The PhoU protein from Escherichia coli interacts with PhoR, PstB, and metals to form a phosphate-signaling complex at the membrane.
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PstC and PstA form the integral inner-membrane pore of the PstSCAB ABC phosphate importer.
"PstS is the periplasmic P i -binding protein, PstC and PstA are integral membrane proteins that form the pore through which P i passes, and PstB is the dimeric, cytoplasmic ATPase."