ID PTPB_STAA3 Reviewed; 139 AA. AC Q2FF13; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Low molecular weight protein-tyrosine-phosphatase PtpB; DE EC=3.1.3.48; DE AltName: Full=Phosphotyrosine phosphatase B; DE Short=PTPase B; GN Name=ptpB; OrderedLocusNames=SAUSA300_2069; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). 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; CP000255; ABD21952.1; -; Genomic_DNA. DR RefSeq; WP_000697334.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FF13; -. DR SMR; Q2FF13; -. DR KEGG; saa:SAUSA300_2069; -. DR HOGENOM; CLU_071415_1_2_9; -. DR Proteomes; UP000001939; Chromosome. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd16344; LMWPAP; 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; LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE; 1. DR PANTHER; PTHR11717:SF31; LOW MOLECULAR WEIGHT PROTEIN-TYROSINE-PHOSPHATASE PTPB; 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..139 FT /note="Low molecular weight protein-tyrosine-phosphatase FT PtpB" FT /id="PRO_0000300679" FT ACT_SITE 7 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P11064" FT ACT_SITE 13 FT /evidence="ECO:0000250|UniProtKB:P11064" FT ACT_SITE 111 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P11064" SQ SEQUENCE 139 AA; 15788 MW; 63EB2C0E2A53EA5B CRC64; MKILFVCTGN TCRSPLAESI AKEVMPNHQF ESRGIFAVNN QGVSNYVEDL VEEHHLAETT LSQQFTEADL KADIILTMSY SHKELIEAHF GLQNHVFTLH EYVKEAGEVI DPYGGTKEMY VHTYEELVSL ILKLKDIIC //