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
UniProtKB record A0A0H2MBK2 (A0A0H2MBK2_VARPD) - Phosphate-specific transport system accessory protein PhoU from Variovorax paradoxus TBEA6
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VPARA_10440 (phoU, A0A0H2MBK2) is a 233-aa cytoplasmic homodimer (InterPro IPR028366, NCBIfam TIGR02135, PIRSF PIRSF003107, PANTHER PTHR42930:SF3) containing two tandem PhoU three-helix bundle domains (Pfam PF01895 at residues 22-108 and 129-210).
"CC -!- FUNCTION: Plays a role in the regulation of phosphate uptake.
CC {ECO:0000256|PIRNR:PIRNR003107}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR003107}."
Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships.
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Establishes the sequence and organization of phoU at the 3' end of 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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PhoU is a soluble homodimer that binds Mn(2+) and Mg(2+) at conserved three-helix bundle sites (which may be important for PhoU membrane interactions) and physically interacts with both PstB and the PAS domain of PhoR.
"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. We have also shown that the soluble form of PhoU is a dimer that binds manganese and magnesium."