Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885).
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Purified TpbA hydrolyses pNPP and phosphotyrosine peptides; activity is vanadate-sensitive.
"TpbA-cHis dephosphorylated both phosphotyrosine peptides"
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TpbA is periplasmic by fractionation.
"we found that TpbA exclusively localized in the periplasm"
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Model: periplasmic TpbA dephosphorylates TpbB to lower c-di-GMP.
"Periplasmic TpbA dephosphorylates the membrane-anchored GGDEF protein TpbB at a tyrosine reside which deactivates GGDEF protein activity"
Structural and Biochemical Analysis of Tyrosine Phosphatase Related to Biofilm Formation A (TpbA) from the Opportunistic Pathogen Pseudomonas aeruginosa PAO1.
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PAO1 TpbA structures and peptide assays; prefers TpbB pTyr48.
"TpbA efficiently catalyzes the hydrolysis of two phosphotyrosine peptides derived from the periplasmic domain of TpbB"
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TpbA can dephosphorylate pTyr, pSer and pThr.
"has been shown to possess phosphatase activities for pNPP and phosphotyrosine peptides, and can dephosphorylate pTyr, pSer and pThr residues"
Gene Ontology annotation based on Enzyme Commission mapping
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt