ID   SPTP_SALPA              Reviewed;         543 AA.
AC   Q5PEA9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
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; OrderedLocusNames=SPA2736;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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       T3SS), 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; CP000026; AAV78593.1; -; Genomic_DNA.
DR   RefSeq; WP_000946993.1; NC_006511.1.
DR   AlphaFoldDB; Q5PEA9; -.
DR   SMR; Q5PEA9; -.
DR   KEGG; spt:SPA2736; -.
DR   HOGENOM; CLU_039619_0_0_6; -.
DR   Proteomes; UP000008185; 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:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14559; PTP_YopH-like; 1.
DR   CDD; cd00219; ToxGAP; 1.
DR   Gene3D; 4.10.1330.10; non globular Virulence effector SptP domain; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 1.20.120.260; Virulence factor YopE uncharacterised domain; 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   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF527; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 7; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF47233; Bacterial GAP domain; 1.
DR   SUPFAM; SSF56568; Non-globular alpha+beta subunits of globular proteins; 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_0000094864"
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;  60005 MW;  BE20AFE173E8C1D3 CRC64;
     MLRYEERKLN NLTLSSFSKS GVSSDTRLYI AKENTDKAYV APEKFSSKVL TWLGKMPLFK
     NTEVVQKHTE NIRVQNQKIL QTFLQALTEK YGEKAVNNAL YMSSINMNKP LTQRLVVQIT
     ECVKGADGGF INIIKNKDNV GVMNAALVIK GGDTKVTEQN NDVGAESKQP LLDIALKGLK
     RTIPQLEQMD GNSLRENFQE MASGNGPLRS LMTNLQSLNK IPEAKQLNDY VTTLKNIQIG
     ADRFSQWGTC GGEVERWIDK ASTHELTQAV KKIHVIAKEL KNVTAEFEKI KAGASMPQTM
     NGPTLGLARF AVSSIPINQQ TQVKLSDGMP VPVNTLTFDG KPVALAGSYP KNTPDALEAH
     MKMLLEKECS CLAVLTSEDQ MQAKQLPAYF RGSYTFGEVH TNSQKVSSAS QGGAIDQYNM
     QLSCGEKRYT IPVLHVKNWP DHQPLPSTDQ LEYLADRVKN SNQNGAPGRS SSDKHLPMIH
     CLGGVGRTGT MAAALVLKDN PHSNLEQVRA DFRNSRNNRM LEDASQFVQL KAMQAQLLMT
     TAS
//