ID PTPA_STAES Reviewed; 154 AA. AC Q8CNQ1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Low molecular weight protein-tyrosine-phosphatase PtpA; DE EC=3.1.3.48; DE AltName: Full=Phosphotyrosine phosphatase A; DE Short=PTPase A; GN Name=ptpA; OrderedLocusNames=SE_1566; OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12228 / FDA PCI 1200; RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). CC -!- FUNCTION: Dephosphorylates the phosphotyrosine-containing proteins. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein CC phosphatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE015929; AAO05165.1; -; Genomic_DNA. DR RefSeq; NP_765121.1; NC_004461.1. DR RefSeq; WP_001830437.1; NZ_WBME01000010.1. DR AlphaFoldDB; Q8CNQ1; -. DR SMR; Q8CNQ1; -. DR GeneID; 50018334; -. DR KEGG; sep:SE_1566; -. DR PATRIC; fig|176280.10.peg.1530; -. DR eggNOG; COG0394; Bacteria. DR HOGENOM; CLU_071415_2_3_9; -. DR OrthoDB; 9784339at2; -. DR Proteomes; UP000001411; Chromosome. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd16343; LMWPTP; 1. DR Gene3D; 3.40.50.2300; -; 1. DR InterPro; IPR023485; Ptyr_pPase. DR InterPro; IPR036196; Ptyr_pPase_sf. DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt. DR PANTHER; PTHR11717:SF7; LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11717; LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE; 1. DR Pfam; PF01451; LMWPc; 1. DR PRINTS; PR00719; LMWPTPASE. DR SMART; SM00226; LMWPc; 1. DR SUPFAM; SSF52788; Phosphotyrosine protein phosphatases I; 1. PE 3: Inferred from homology; KW Hydrolase; Protein phosphatase. FT CHAIN 1..154 FT /note="Low molecular weight protein-tyrosine-phosphatase FT PtpA" FT /id="PRO_0000300666" FT ACT_SITE 8 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P11064" FT ACT_SITE 14 FT /evidence="ECO:0000250|UniProtKB:P11064" FT ACT_SITE 120 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P11064" SQ SEQUENCE 154 AA; 17760 MW; AE9E2583CFE9A7DE CRC64; MIHVAFVCLG NICRSPMAEA IMRQRLQERG ISDIKVHSRG TGRWNLGEPP HNGTQKILQK YHIPYDGMVS ELFEPDDDFD YIIAMDQSNV DNIKQINPNL QGQLFKLLEF SNMEESDVPD PYYTNNFEGV FEMVQSSCDN LIDYIVKDAN LKER //