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PTPA_STAAM
ID   PTPA_STAAM              Reviewed;         154 AA.
AC   Q99T00;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=SAV1881;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
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: Secreted tyrosine phosphatase that plays a critical role
CC       during infection as a bacterial effector protein that counteracts host
CC       defenses. Required for intramacrophage survival.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
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         Evidence={ECO:0000250|UniProtKB:A0A0H3K9F2};
CC   -!- SUBUNIT: Interacts with host CORO1A.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC       Note=Secreted intracellularly upon bacterial infection of macrophages.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- PTM: Phosophorylations at Tyr-122 and Tyr-123 are essential for
CC       phosphatase activity. {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB58043.1; -; Genomic_DNA.
DR   RefSeq; WP_000228666.1; NC_002758.2.
DR   AlphaFoldDB; Q99T00; -.
DR   SMR; Q99T00; -.
DR   PaxDb; Q99T00; -.
DR   EnsemblBacteria; BAB58043; BAB58043; SAV1881.
DR   KEGG; sav:SAV1881; -.
DR   HOGENOM; CLU_071415_2_3_9; -.
DR   OMA; TGSWHVG; -.
DR   PhylomeDB; Q99T00; -.
DR   BioCyc; SAUR158878:SAV_RS10295-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Phosphoprotein; Protein phosphatase; Secreted.
FT   CHAIN           1..154
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   PtpA"
FT                   /id="PRO_0000300661"
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;  17491 MW;  67E81E0B8125B1E8 CRC64;
     MVDVAFVCLG NICRSPMAEA IMRQRLKDRN IHDIKVHSRG TGSWNLGEPP HEGTQKILNK
     HNIPFDGMIS ELFEATDDFD YIVAMDQSNV DNIKSINPNL KGQLFKLLEF SNMEESDVPD
     PYYTNNFEGV YDMVLSSCDN LIDYIVKDAN LKEG
 
 
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