ID   SOPB_SALBN              Reviewed;         416 AA.
AC   Q9AH17;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 50.
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 bongori.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=54736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SARC11;
RX   PubMed=11244077; DOI=10.1128/jb.183.7.2348-2358.2001;
RA   Mirold S., Ehrbar K., Weissmueller A., Prager R., Tschaepe H.,
RA   Ruessmann H., Hardt W.-D.;
RT   "Salmonella host cell invasion emerged by acquisition of a mosaic of
RT   separate genetic elements, including Salmonella pathogenicity island 1
RT   (SPI1), SPI5, and sopE2.";
RL   J. Bacteriol. 183:2348-2358(2001).
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; AF323079; AAK27357.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AH17; -.
DR   SMR; Q9AH17; -.
DR   STRING; 218493.SBG_0939; -.
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..416
FT                   /note="Inositol phosphate phosphatase SopB"
FT                   /id="PRO_0000220490"
FT   MOTIF           315..321
FT                   /note="CX5R motif"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   416 AA;  45795 MW;  390798A6F83CAA3D CRC64;
     PAQEAHQVAV AAFREAQVQY LNNQPWQTIK NTLTHNGYRY TNTQCPAADM KIGAQDIFPN
     AYQGKGVCSS DTTNTQHATN LWMSTLSVNE NGKDKTLFCG IRHGVLSPYH VKDPILRQVG
     AENRAREVLT AALFSQPALL TKALQDEVVS LRLVSVGLLT TSTIVGNEDA MVQDQMRAWQ
     SLTQPGNVIH LNIRNKEGEL RTVKIKPEIA AFNTGVNELT LKLGLGHQAS DNYNIGALHQ
     LLGHDLRPEA PPGGWVGEWL AQHPDNHAVV NTLVRQIKDI WNSKLHHTDG NEPYKFAQRL
     AILAHEIGAV PAWNCKSGKD RTGMQDAEIK REVISLHQKA TLTPLASLPD SDGQEIFQKV
     LLNSGNLEIQ KQNTGGAGNK VLKNLPPEVL NLSYQRRIGD ANIWQLVKGL SSLVTS