Gene Ontology annotation through association of InterPro records with GO terms
UniProtKB record A0A0H2M7F6 (A0A0H2M7F6_VARPD) - Phosphate-binding protein PstS from Variovorax paradoxus TBEA6
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VPARA_10480 (pstS, A0A0H2M7F6) is a 345-aa periplasmic phosphate-binding protein (InterPro IPR005673, CDD cd13565, Pfam PF12849, NCBIfam TIGR00975, PANTHER PTHR42996:SF1) with an N-terminal SignalP signal peptide (residues 1-24) and mature periplasmic chain (residues 25-345).
"FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..345
FT /note="Phosphate-binding protein PstS"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002596677"
FT DOMAIN 26..304
FT /note="PBP"
FT /evidence="ECO:0000259|Pfam:PF12849""
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PstS is the solute-binding subunit of the PstSACB ABC phosphate importer complex encoded on contig JZWI01000005 (KLN58036.1).
"CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PstB),
CC two transmembrane proteins (PstC and PstA) and a solute-binding protein
CC (PstS). {ECO:0000256|ARBA:ARBA00011529, ECO:0000256|PIRNR:PIRNR002756}."
High specificity of a phosphate transport protein determined by hydrogen bonds.
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High-resolution (1.7 A) crystal structure of bacterial periplasmic phosphate-binding protein (PstS) reveals the atomic features responsible for orthophosphate selectivity and exclusion of sulfate.
"We report here the highly refined 1.7 A resolution X-ray structure of the liganded form of the phosphate-binding protein. The structure reveals the atomic features responsible for phosphate selectivity, either in monobasic or dibasic form, and the exclusion of sulphate."
Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene.
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Establishes that phoS (pstS) encodes the periplasmic phosphate-binding protein exported via a cleavable N-terminal signal sequence.
"The complete nucleotide sequence of the phoS gene, the structural gene for the phosphate-repressible, periplasmic phosphate-binding protein Escherichia coli K-12, was determined. The phosphate-binding protein is synthesized in a precursor form which includes an additional N-terminal segment containing 25 amino acid residues, with the general characteristics of a signal sequence."
Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships.
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Determines the complete sequence and gene-polypeptide organization of the phoS (pstS)-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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Synthesizes the subunit architecture and signaling role of the PstSCAB type I ABC phosphate importer and its coupling through PhoU to PhoR-PhoB.
"The Pst proteins form a type I ATP-binding cassette (ABC) importer that exhibits high-affinity, P i -specific transport ( 18 – 20 ). 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."