ID   SOPB_SALTI              Reviewed;         561 AA.
AC   Q8Z7R1; Q7C973; Q9RER3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Inositol phosphate phosphatase SopB;
DE            EC=3.1.3.-;
DE   AltName: Full=Effector protein SopB;
GN   Name=sopB; Synonyms=sigD; OrderedLocusNames=STY1121, t1828;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
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   [2]
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-529.
RC   STRAIN=IE1537;
RX   PubMed=11200542; DOI=10.1016/s1438-4221(00)80009-0;
RA   Prager R., Mirold S., Tietze E., Strutz U., Knuppel B., Rabsch W.,
RA   Hardt W.-D., Tschape H.;
RT   "Prevalence and polymorphism of genes encoding translocated effector
RT   proteins among clinical isolates of Salmonella enterica.";
RL   Int. J. Med. Microbiol. 290:605-617(2000).
CC   -!- FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns
CC       3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to
CC       PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella
CC       into the host cell and is required for invasion and for an efficient
CC       generation and maintenance of Salmonella-containing vacuole (SVC).
CC       Alteration of the phosphoinositide composition of the plasma membrane
CC       causes membrane ruffling and actin cytoskeleton rearrangements. The
CC       persistence of PtdIns 3-P diverts the SCV from the endocytic pathway
CC       resulting in enlarged vesicles, which are essential to create a
CC       favorable environment where Salmonella can replicate and avoid immune
CC       defenses of the host cell (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted via the
CC       type III secretion system 1 (SPI-1 TTSS). {ECO:0000250}.
CC   -!- DOMAIN: Contains the consensus sequence Cys-X(5)-Arg characteristic of
CC       Mg-independent phosphatases. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphatase IpgD/SopB family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD08217.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69449.1; -; Genomic_DNA.
DR   EMBL; AF213333; AAF21055.1; -; Genomic_DNA.
DR   RefSeq; NP_455588.1; NC_003198.1.
DR   RefSeq; WP_001166955.1; NZ_WSUR01000018.1.
DR   AlphaFoldDB; Q8Z7R1; -.
DR   SMR; Q8Z7R1; -.
DR   STRING; 220341.16502265; -.
DR   EnsemblBacteria; AAO69449; AAO69449; t1828.
DR   KEGG; stt:t1828; -.
DR   KEGG; sty:STY1121; -.
DR   PATRIC; fig|220341.7.peg.1124; -.
DR   eggNOG; ENOG502Z7Z8; Bacteria.
DR   HOGENOM; CLU_025781_0_0_6; -.
DR   OMA; CWNCKSG; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   InterPro; IPR008108; IpgD/SopB.
DR   Pfam; PF05925; IpgD; 1.
DR   PRINTS; PR01734; TYPE3OMBPROT.
PE   3: Inferred from homology;
KW   Hydrolase; Secreted; Virulence.
FT   CHAIN           1..561
FT                   /note="Inositol phosphate phosphatase SopB"
FT                   /id="PRO_0000220494"
FT   MOTIF           460..466
FT                   /note="CX5R motif"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000305"
FT   CONFLICT        528
FT                   /note="K -> H (in Ref. 3; AAF21055)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   561 AA;  62017 MW;  774057AE49A0BF2D CRC64;
     MQIQSFYHSA SLKTQEAFKS LQKTLYNGMQ ILSGQGKAPA KAPDARPEII VLREPGATWG
     NYLQHQKTSN HSLHNLYNLQ RDLLTVAATV LGKQDPVLTS MANQMELAKV KADRPATKQE
     EAAAKALKKN LIELIAARTQ QQNGLPAKEA HRFAAVAFRD AQVKQLNNQP WQTIKNTLTH
     NGHHYTNTQL PAAEMKIGAK DIFPSAYEGK GVCSWDTKNI HHANNLWMST VSVHEDGKDK
     TLFCGIRHGV LSPYHEKDPL LRQAGAENKA KEVLAAALFS KPELLNRALE GEAVSLKLVS
     VGLLTASNIF GKEGTMVEDQ MRAWQSLTQP GKMIHLKIRN KDGDLQTVKI KPDVAAFNVG
     VNELALKLGF GLKASDSYNA EALHQLLGND LRPEARPGGW VGEWLAQYPD NYEVVNTLAR
     QIKDIWKNNQ HHKDGGEPYK LAQRLAMLAH EIDAVPAWNC KSGKDRTGMM DSEIKRELIS
     FHQTHMLSAP GSLPDSGGQK IFQKVLLNSG NLEIQKQNTG GAGNKVMKNL SPEVLNLSYQ
     KRVGDENIWQ SVKGISSLIT S