ID   PTPB_STAAN              Reviewed;         139 AA.
AC   Q7A4E1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=SA1917;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB43201.1; -; Genomic_DNA.
DR   PIR; H90004; H90004.
DR   RefSeq; WP_000697334.1; NC_002745.2.
DR   AlphaFoldDB; Q7A4E1; -.
DR   SMR; Q7A4E1; -.
DR   EnsemblBacteria; BAB43201; BAB43201; BAB43201.
DR   KEGG; sau:SA1917; -.
DR   HOGENOM; CLU_071415_1_2_9; -.
DR   Proteomes; UP000000751; 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_0000300677"
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
//