ID   SOPB_SALBL              Reviewed;         433 AA.
AC   Q9RER2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Inositol phosphate phosphatase SopB;
DE            EC=3.1.3.-;
DE   AltName: Full=Effector protein SopB;
DE   Flags: Fragment;
GN   Name=sopB; Synonyms=sigD;
OS   Salmonella blockley.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=57741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IE1536;
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.
CC   -!- SIMILARITY: Belongs to the phosphatase IpgD/SopB family. {ECO:0000305}.
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DR   EMBL; AF213334; AAF21056.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RER2; -.
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..>433
FT                   /note="Inositol phosphate phosphatase SopB"
FT                   /id="PRO_0000220489"
FT   MOTIF           364..370
FT                   /note="CX5R motif"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         433
SQ   SEQUENCE   433 AA;  47750 MW;  7C3F886F37269A4A CRC64;
     VLTSMANQME LAKVKADRPA TKQEEAAAKA LKKNLIELIA ARTQQQDGLP AKEAHRFAAV
     AFRDAQVKQL NNQPWQTIKN TLTHNGHHYT NTQLPAAEMK IGAKDIFPSA YEGKGVCSWD
     TKNIHHANNL WMSTVSVHED GKDKTLFCGI RHGVLSPYHE KDPLLRQVGA ENKAKEVLTA
     ALFSKPELLN KALAGEAVSL KLVSVGLLTA SNIFGKEGTM VEDQMRAWQS LTQPGKMIHL
     KIRNKDGDLQ TVKIKPDVAA FNVGVNELAL KLGFGLKASD SYNAEALHQL LGNDLRPEAR
     PGGWVGEWLA QYPDNYEVVN TLARQIKDIW KNNQHHKDGG EPYKLAQRLA MLAHEIDAVP
     AWNCKSGKDR TGMMDSEIKR EHISLHQTHM LSAPGSLPDS GGQKIFQKVL LNSGNLEIQK
     QNTGGAGNKV MKN