PTPA_STAAE
ID PTPA_STAAE Reviewed; 154 AA.
AC A0A0H3K9F2;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 30.
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=NWMN_1819;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP PHOSPHORYLATION AT TYR-122 AND TYR-123, MUTAGENESIS OF ASP-120; TYR-122 AND
RP TYR-123, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RC STRAIN=Newman;
RX PubMed=26679607; DOI=10.1016/j.bbrc.2015.11.123;
RA Brelle S., Baronian G., Huc-Brandt S., Zaki L.G., Cohen-Gonsaud M.,
RA Bischoff M., Molle V.;
RT "Phosphorylation-mediated regulation of the Staphylococcus aureus secreted
RT tyrosine phosphatase PtpA.";
RL Biochem. Biophys. Res. Commun. 469:619-625(2016).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST CORO1A, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Newman;
RX PubMed=30131335; DOI=10.1074/jbc.ra118.003555;
RA Gannoun-Zaki L., Paetzold L., Huc-Brandt S., Baronian G., Elhawy M.I.,
RA Gaupp R., Martin M., Blanc-Potard A.B., Letourneur F., Bischoff M.,
RA Molle V.;
RT "PtpA, a secreted tyrosine phosphatase from Staphylococcus aureus,
RT contributes to virulence and interacts with coronin-1A during infection.";
RL J. Biol. Chem. 293:15569-15580(2018).
CC -!- FUNCTION: Staphylococcal enterotoxin that activates the host immune
CC system by binding as unprocessed molecules to major histocompatibility
CC (MHC) complex class II and T-cell receptor (TCR) molecules. In turn,
CC waves of cellular activation, cytokine production, and migration into
CC the lung tissue and airways occur via alphabeta T-cells. Causes also
CC the intoxication staphylococcal food poisoning syndrome. The illness is
CC characterized by high fever, hypotension, diarrhea, shock, and in some
CC cases death. {ECO:0000250|UniProtKB:P0A0L2}.
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:0000269|PubMed:26679607};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A0L2};
CC Note=Binds 1 zinc ion per subunit. The zinc ion is necessary for the
CC toxin interaction with MHC class II. {ECO:0000250|UniProtKB:P0A0L2};
CC -!- SUBUNIT: Monomer. Interacts with MHC class II molecules alpha/HLA-DRB1
CC and beta/HLA-DRA chains. The interaction with MHC-II molecules occurs
CC at both zinc-dependent and zinc-independent sites. Interacts with T-
CC cell receptor beta variable 7-9/TRBV7-9.
CC {ECO:0000250|UniProtKB:P0A0L2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0A0L2}.
CC -!- PTM: Phosophorylations at Tyr-122 and Tyr-123 are essential for
CC phosphatase activity. {ECO:0000269|PubMed:26679607}.
CC -!- DISRUPTION PHENOTYPE: Loss of about 70% of intramacrophage survival.
CC {ECO:0000269|PubMed:30131335}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; AP009351; BAF68091.1; -; Genomic_DNA.
DR RefSeq; WP_000228666.1; NZ_CP023390.1.
DR AlphaFoldDB; A0A0H3K9F2; -.
DR SMR; A0A0H3K9F2; -.
DR iPTMnet; A0A0H3K9F2; -.
DR EnsemblBacteria; BAF68091; BAF68091; NWMN_1819.
DR KEGG; sae:NWMN_1819; -.
DR HOGENOM; CLU_071415_2_3_9; -.
DR OMA; TGSWHVG; -.
DR Proteomes; UP000006386; 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 1: Evidence at protein level;
KW Hydrolase; Phosphoprotein; Protein phosphatase; Secreted.
FT CHAIN 1..154
FT /note="Low molecular weight protein-tyrosine-phosphatase
FT PtpA"
FT /id="PRO_0000447641"
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"
FT MOD_RES 122
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26679607"
FT MOD_RES 123
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26679607"
FT MUTAGEN 120
FT /note="D->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:26679607"
FT MUTAGEN 122
FT /note="Y->A: Complete loss of activity; in association with
FT A-123."
FT /evidence="ECO:0000269|PubMed:26679607"
FT MUTAGEN 123
FT /note="Y->A: Complete loss of activity; in association with
FT A-122."
FT /evidence="ECO:0000269|PubMed:26679607"
SQ SEQUENCE 154 AA; 17491 MW; 67E81E0B8125B1E8 CRC64;
MVDVAFVCLG NICRSPMAEA IMRQRLKDRN IHDIKVHSRG TGSWNLGEPP HEGTQKILNK
HNIPFDGMIS ELFEATDDFD YIVAMDQSNV DNIKSINPNL KGQLFKLLEF SNMEESDVPD
PYYTNNFEGV YDMVLSSCDN LIDYIVKDAN LKEG
