PTPA_STAHJ
ID PTPA_STAHJ Reviewed; 154 AA.
AC Q4L7J1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=SH1075;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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}.
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DR EMBL; AP006716; BAE04384.1; -; Genomic_DNA.
DR RefSeq; WP_011275379.1; NC_007168.1.
DR AlphaFoldDB; Q4L7J1; -.
DR SMR; Q4L7J1; -.
DR STRING; 279808.SH1075; -.
DR EnsemblBacteria; BAE04384; BAE04384; SH1075.
DR GeneID; 58062752; -.
DR KEGG; sha:SH1075; -.
DR eggNOG; COG0394; Bacteria.
DR HOGENOM; CLU_071415_2_3_9; -.
DR OMA; TGSWHVG; -.
DR OrthoDB; 2062716at2; -.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 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_0000300668"
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; 17450 MW; 2B73F64676E5D9AE CRC64;
MVDVAFVCLG NICRSPMAEA IMRQRLIDRN ISGVNVYSKG TGKWNLGEPP HEGTQDILNR
HNIPFDGMIS ELFESSDDFD YIIAMDQSNV DNIQNINPNI KGKLFKLLEF SNMEESDVPD
PYYTNNFEGV YEMVQSSCDN LIDFIVKDAN LKEG