ID   SPTP_SALTI              Reviewed;         543 AA.
AC   P74851; Q7AME2; Q7C7N7;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Secreted effector protein SptP;
DE   Includes:
DE     RecName: Full=GTPase-activating protein;
DE              Short=GAP;
DE   Includes:
DE     RecName: Full=Tyrosine-protein phosphatase;
DE              EC=3.1.3.48;
GN   Name=sptP; Synonyms=stpA; OrderedLocusNames=STY3001, t2780;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=9404501; DOI=10.1016/s0923-2508(97)81896-7;
RA   Arricau N., Hermant D., Waxin H., Popoff M.Y.;
RT   "Molecular characterization of the Salmonella typhi StpA protein that is
RT   related to both Yersinia YopE cytotoxin and YopH tyrosine phosphatase.";
RL   Res. Microbiol. 148:21-26(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC       promote bacterial survival in host tissues. This protein includes
CC       tyrosine phosphatase and GTPase activating protein (GAP) activities.
CC       After bacterial internalization, GAP mediates the reversal of the
CC       cytoskeletal changes induced by SopE. This function is independent of
CC       its tyrosine phosphatase activity, which remains unclear (By
CC       similarity). {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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- SUBUNIT: Forms a complex with SicP. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=Secreted via type III secretion system 1 (SPI-1
CC       TTSS), and delivered into the host cytoplasm. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Requires SicP as a chaperone for its stability and
CC       secretion. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the YopE family.
CC       {ECO:0000305}.
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DR   EMBL; X92546; CAA63304.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD05985.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70341.1; -; Genomic_DNA.
DR   RefSeq; NP_457272.1; NC_003198.1.
DR   RefSeq; WP_000946989.1; NZ_QXGZ01000003.1.
DR   AlphaFoldDB; P74851; -.
DR   SMR; P74851; -.
DR   STRING; 220341.16503956; -.
DR   EnsemblBacteria; AAO70341; AAO70341; t2780.
DR   KEGG; stt:t2780; -.
DR   KEGG; sty:STY3001; -.
DR   PATRIC; fig|220341.7.peg.3055; -.
DR   eggNOG; COG5599; Bacteria.
DR   HOGENOM; CLU_039619_0_0_6; -.
DR   OMA; WIDKAST; -.
DR   PHI-base; PHI:6798; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   CDD; cd00219; ToxGAP; 1.
DR   Gene3D; 1.20.120.260; -; 1.
DR   Gene3D; 3.90.190.10; -; 1.
DR   Gene3D; 4.10.1330.10; -; 1.
DR   InterPro; IPR011070; Globular_prot_asu/bsu.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR015203; SptP_N.
DR   InterPro; IPR044899; SptP_N_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR003546; Tyr_Pase_SptP/YopH.
DR   InterPro; IPR014773; YopE_GAP_dom.
DR   InterPro; IPR037168; YopE_GAP_dom_sf.
DR   Pfam; PF09119; SicP-binding; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   Pfam; PF03545; YopE; 1.
DR   PRINTS; PR01371; BACYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF47233; SSF47233; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF56568; SSF56568; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   GTPase activation; Host cytoplasm; Hydrolase; Protein phosphatase;
KW   Secreted; Virulence.
FT   CHAIN           1..543
FT                   /note="Secreted effector protein SptP"
FT                   /id="PRO_0000094865"
FT   DOMAIN          280..543
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          35..139
FT                   /note="Chaperone-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          167..290
FT                   /note="GAP"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        481
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
SQ   SEQUENCE   543 AA;  59898 MW;  72E8DAA70ABD9E00 CRC64;
     MLRYDERKLN NLTLSSFSKS GVSSDTRLYI AKENTDKAYV APEKFSSKVL TWLGKMPLFK
     NTEVVQKHTE NIRVQNQKIL QTFLQALTEK YGEKAVNNAL YMSSINMNKP LTQRLVVQIT
     ECVKGADGGF INLIKNKDNV GVMNAALVIK GGDTKVTEQN NDVGAESKQP LLDIALKGLK
     RTIPQLEQMD GNSLRENFQE MASGNGPLRS LMTNLQSLNK IPEAKQLNDY VTTLKNIQIG
     ADRFSQWGTC GGEVERWIDK ASTHELTQAV KKIHVIAKEL KNVTAELEKI KAGASMPQTM
     SGPTLGLARF AVSSIPINQQ TQVKLSDGMP VPVNTLTFDG KPVALAGSCP KNTPDALEAH
     MKMLLEKECS CLVVLTSEDQ MQAKQLPAYF RGSYTFGEVH TNSQKVSSAS QGGAIDQYNM
     QLSCGEKRYT IPVLHVKNWP DHQPLPSTDQ LEYLADRVKN SNQNGAPGRS SSDKHLPMIH
     CLGGVGRTGT MAAALVLKDN PHSNLEQVRA DFRNSRNNRM LEDASQFVQL KAMQAQLLMT
     TAS