ID   PTPB_STAA8              Reviewed;         139 AA.
AC   Q2FWE3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=SAOUHSC_02356;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (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; CP000253; ABD31387.1; -; Genomic_DNA.
DR   RefSeq; WP_000697334.1; NZ_LS483365.1.
DR   RefSeq; YP_500832.1; NC_007795.1.
DR   AlphaFoldDB; Q2FWE3; -.
DR   SMR; Q2FWE3; -.
DR   STRING; 93061.SAOUHSC_02356; -.
DR   PaxDb; 1280-SAXN108_2360; -.
DR   GeneID; 3919399; -.
DR   KEGG; sao:SAOUHSC_02356; -.
DR   PATRIC; fig|93061.5.peg.2133; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_1_2_9; -.
DR   OrthoDB; 9784339at2; -.
DR   PHI-base; PHI:11296; -.
DR   PHI-base; PHI:11719; -.
DR   PRO; PR:Q2FWE3; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..139
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   PtpB"
FT                   /id="PRO_0000300678"
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
//