Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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 A0A0D0L7E0 (A0A0D0L7E0_VARPD) - Phosphate import ATP-binding protein PstB from Variovorax paradoxus TBEA6
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VPARA_10450 (pstB, A0A0D0L7E0) is a 259-aa peripheral inner-membrane ABC ATPase subunit (InterPro IPR005670, CDD cd03260, NCBIfam TIGR00972, PANTHER PTHR43423:SF3, PROSITE PS50893) with a Walker A ATP-binding site at residues 45-52 (45-GPSGCGKS-52).
"FT DOMAIN 13..254
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434""
Specific amino acid residues in both the PstB and PstC proteins are required for phosphate transport by the Escherichia coli Pst system.
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Substitutions at Walker A residues Gly48 and Lys49 in E. coli PstB (corresponding to Gly50 and Lys51 in VPARA_10450) abolish phosphate transport through the Pst system and cause constitutive derepression of alkaline phosphatase.
"The amino acid substitutions Gly-48----Ile and Lys-49----Gln, resulting from the pstB mutations, caused the loss of phosphate transport through the Pst system and the derepression of alkaline phosphatase activity. The residues Gly-48 and Lys-49 are key residues in the putative nucleotide-binding site."
Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships.
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Establishes the sequence and organization of pstB 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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PstB is the dimeric cytoplasmic ATPase of the PstSCAB importer and directly interacts with PhoU to form the membrane-associated phosphate signaling complex.
"We have demonstrated using bacterial two-hybrid analysis and confirmatory coelution experiments that PhoU interacts with PhoR through its PAS (Per-ARNT-Sim) domain and that it also interacts with PstB, the cytoplasmic component of the transporter."