SPTP_SALPA
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 03-AUG-2022, entry version 98.
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; Proteobacteria; 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 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; CP000026; AAV78593.1; -; Genomic_DNA.
DR RefSeq; WP_000946993.1; NC_006511.1.
DR AlphaFoldDB; Q5PEA9; -.
DR SMR; Q5PEA9; -.
DR EnsemblBacteria; AAV78593; AAV78593; SPA2736.
DR KEGG; spt:SPA2736; -.
DR HOGENOM; CLU_039619_0_0_6; -.
DR OMA; WIDKAST; -.
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: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_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
