ID   SOPB_SALHO              Reviewed;         416 AA.
AC   Q9AH18;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 44.
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 houtenae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=59205;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SARC10 / s3027;
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; AF323078; AAK27356.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AH18; -.
DR   SMR; Q9AH18; -.
DR   STRING; 523831.SEHO0A_00976; -.
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_0000220493"
FT   MOTIF           315..321
FT                   /note="CX5R motif"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   416 AA;  46097 MW;  AF55172AF8AFEAFF CRC64;
     PAKEARRLAA ADFKSAQVKQ LNNQPWQTIK NTLTHNGHQY TSTQVPAAEM KIGAQDIFPK
     AYQGKGVCSW DTQNIHHATN LWMSTISVHE DGEDKTLFSG IRHGVLSPYH VEDPLLRQTG
     AESRAKEVLT AALFSKPELL TRALKGEAVS LKLVSVCLLT ASNVLGQEGT MVKEQMRAWQ
     SLTQPGKMIH LKIRNDDGEL QTVKIKPEVA AFNVGVNELA LKFGFGLKAS DSYNIEALQQ
     LLGNDLRPEA RPGGWVGEWL ARYPDNDESV NTLARQIKDI WQNKLHHKDG GEPYKLAQRL
     AMLANEIDVV PAWNCKSGKD RTGMMDSETK REAISFHQTH TLSSPGSLPD RSGQQIFQKV
     LLNSGNLEIQ KQNTSGAGNK VIKNLSPEVL NLSYHKRIGD ENTWQSVKGI STLIIS