ID   SOPB_SALDU              Reviewed;         561 AA.
AC   O34105; Q9L6X6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Inositol phosphate phosphatase SopB;
DE            EC=3.1.3.-;
DE   AltName: Full=Effector protein SopB;
GN   Name=sopB; Synonyms=sigD;
OS   Salmonella dublin.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=98360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15 AND 55-67, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=2229;
RX   PubMed=9364916; DOI=10.1111/j.1365-2958.1997.mmi525.x;
RA   Galyov E.E., Wood M.W., Rosqvist R., Mullan P.B., Watson P.R., Hedges S.,
RA   Wallis T.S.;
RT   "A secreted effector protein of Salmonella dublin is translocated into
RT   eukaryotic cells and mediates inflammation and fluid secretion in infected
RT   ileal mucosa.";
RL   Mol. Microbiol. 25:903-912(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2229;
RX   PubMed=9723926; DOI=10.1046/j.1365-2958.1998.00984.x;
RA   Wood M.W., Jones M.A., Watson P.R., Hedges S., Wallis T.S., Galyov E.E.;
RT   "Identification of a pathogenicity island required for Salmonella
RT   enteropathogenicity.";
RL   Mol. Microbiol. 29:883-891(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-529.
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).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF CYS-460.
RC   STRAIN=2229;
RX   PubMed=9826652; DOI=10.1073/pnas.95.24.14057;
RA   Norris F.A., Wilson M.P., Wallis T.S., Galyov E.E., Majerus P.W.;
RT   "SopB, a protein required for virulence of Salmonella dublin, is an
RT   inositol phosphate phosphatase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:14057-14059(1998).
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 cells. {ECO:0000269|PubMed:9826652}.
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.
CC   -!- SIMILARITY: Belongs to the phosphatase IpgD/SopB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U90203; AAB68660.1; -; Genomic_DNA.
DR   EMBL; AF060858; AAC33723.1; -; Genomic_DNA.
DR   EMBL; AF231141; AAF43686.1; -; Genomic_DNA.
DR   AlphaFoldDB; O34105; -.
DR   SMR; O34105; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Secreted; Virulence.
FT   CHAIN           1..561
FT                   /note="Inositol phosphate phosphatase SopB"
FT                   /id="PRO_0000220491"
FT   MOTIF           460..466
FT                   /note="CX5R motif"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         460
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9826652"
FT   CONFLICT        163
FT                   /note="D -> V (in Ref. 3; AAF43686)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        512..517
FT                   /note="PGDSEP -> LEIQKQ (in Ref. 3; AAF43686)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   561 AA;  61854 MW;  4B63C42ECA3595D0 CRC64;
     MQIQSFYHSA SLKTQEAFKS LQKTLYNGMQ ILSGQGKAPA KAPDARPEII VLREPGATWG
     NYLQHQKTSN HSLHNLYNLR RDLLTVGATV LGKQDPVLTS MANQMELAKV KADRPATKQE
     EAAAKALKKN LIELIAARTQ QQDGLPAKEA HRFAAVAFRD AQDKQLNNQP WQTIKNTLTH
     NGHHYTNTQL PAAEMKIGAK DIFPSAYEGK GVCSWDTKNI HHANNLWMST VSVHEDGKDK
     TLFCGIRHGV LSPYHEKDPL LRQVGAENKA KEVLTAALFS KPELLNKALA GEAVSLKLVS
     VGLLTASNIF GKEGTMVEDQ MRAWQSLTQP GKMIHLKIRN KDGDLQTVKI KPDVAAFNVG
     VNELALKLGF GLKASDSYNA EALYQLLGND LRPEARPGGW VGEWLAQYPD NYEVVNTLAR
     QIKDIWKNNQ HHKDGGEPYK LAQRLAMLAH EIDAVPAWNC KSGKDRTGMM DSEIKREIIS
     LHQTHMLSAP GSLPDSGGQK IFQKVLLNSG NPGDSEPNTG GAGNKVMKNL SPEVLNLSYQ
     KRVGDENIWQ SVKGISSLIT S