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SOPB_SALTY
ID   SOPB_SALTY              Reviewed;         561 AA.
AC   O30916; Q8ZQ57; Q9L889;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Inositol phosphate phosphatase SopB;
DE            EC=3.1.3.-;
DE   AltName: Full=Effector protein SopB;
GN   Name=sopB; Synonyms=sigD; OrderedLocusNames=STM1091;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=9537377; DOI=10.1128/jb.180.7.1793-1802.1998;
RA   Hong K.H., Miller V.L.;
RT   "Identification of a novel Salmonella invasion locus homologous to Shigella
RT   ipgDE.";
RL   J. Bacteriol. 180:1793-1802(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-529.
RC   STRAIN=IE1534;
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   ROLE IN HOST CELL INVASION, AND SUBCELLULAR LOCATION.
RC   STRAIN=SL1344;
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).
RN   [5]
RP   FUNCTION.
RX   PubMed=11136447; DOI=10.1046/j.1365-2958.2001.02230.x;
RA   Zhou D., Chen L.-M., Hernandez L.D., Shears S.B., Galan J.E.;
RT   "A Salmonella inositol polyphosphatase acts in conjunction with other
RT   bacterial effectors to promote host cell actin cytoskeleton rearrangements
RT   and bacterial internalization.";
RL   Mol. Microbiol. 39:248-259(2001).
RN   [6]
RP   FUNCTION.
RC   STRAIN=SLI344;
RX   PubMed=12360287; DOI=10.1038/ncb854;
RA   Terebiznik M.R., Vieira O.V., Marcus S.L., Slade A., Yip C.M.,
RA   Trimble W.S., Meyer T., Finlay B.B., Grinstein S.;
RT   "Elimination of host cell PtdIns(4,5)P(2) by bacterial SigD promotes
RT   membrane fission during invasion by Salmonella.";
RL   Nat. Cell Biol. 4:766-773(2002).
RN   [7]
RP   FUNCTION.
RX   PubMed=15205533; DOI=10.1126/science.1098188;
RA   Hernandez L.D., Hueffer K., Wenk M.R., Galan J.E.;
RT   "Salmonella modulates vesicular traffic by altering phosphoinositide
RT   metabolism.";
RL   Science 304:1805-1807(2004).
RN   [8]
RP   MUTAGENESIS OF CYS-460; LYS-525 AND LYS-528.
RX   PubMed=11311241; DOI=10.1016/s0014-5793(01)02356-0;
RA   Marcus S.L., Wenk M.R., Steele-Mortimer O., Finlay B.B.;
RT   "A synaptojanin-homologous region of Salmonella typhimurium SigD is
RT   essential for inositol phosphatase activity and Akt activation.";
RL   FEBS Lett. 494:201-207(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. {ECO:0000269|PubMed:11136447,
CC       ECO:0000269|PubMed:11244077, ECO:0000269|PubMed:12360287,
CC       ECO:0000269|PubMed:15205533}.
CC   -!- INTERACTION:
CC       O30916; P60953: CDC42; Xeno; NbExp=5; IntAct=EBI-11167349, EBI-81752;
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; AF021817; AAC46234.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20023.1; -; Genomic_DNA.
DR   EMBL; AF213335; AAF21057.2; -; Genomic_DNA.
DR   RefSeq; NP_460064.1; NC_003197.2.
DR   RefSeq; WP_001166946.1; NC_003197.2.
DR   PDB; 4DID; X-ray; 2.35 A; B=30-181.
DR   PDBsum; 4DID; -.
DR   AlphaFoldDB; O30916; -.
DR   SMR; O30916; -.
DR   IntAct; O30916; 1.
DR   STRING; 99287.STM1091; -.
DR   PaxDb; O30916; -.
DR   EnsemblBacteria; AAL20023; AAL20023; STM1091.
DR   GeneID; 1252609; -.
DR   KEGG; stm:STM1091; -.
DR   PATRIC; fig|99287.12.peg.1155; -.
DR   HOGENOM; CLU_025781_0_0_6; -.
DR   OMA; CWNCKSG; -.
DR   BioCyc; MetaCyc:MON-15186; -.
DR   BioCyc; SENT99287:STM1091-MON; -.
DR   BRENDA; 3.1.3.78; 5542.
DR   PHI-base; PHI:6738; -.
DR   PHI-base; PHI:7236; -.
DR   PHI-base; PHI:7920; -.
DR   PHI-base; PHI:8298; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0071944; C:cell periphery; IMP:AgBase.
DR   GO; GO:0020003; C:symbiont-containing vacuole; IDA:AgBase.
DR   GO; GO:0042577; F:lipid phosphatase activity; IMP:AgBase.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:AgBase.
DR   GO; GO:0023057; P:negative regulation of signaling; IMP:AgBase.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:AgBase.
DR   GO; GO:0045859; P:regulation of protein kinase activity; IMP:AgBase.
DR   DisProt; DP01166; -.
DR   InterPro; IPR008108; IpgD/SopB.
DR   Pfam; PF05925; IpgD; 1.
DR   PRINTS; PR01734; TYPE3OMBPROT.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome; Secreted; Virulence.
FT   CHAIN           1..561
FT                   /note="Inositol phosphate phosphatase SopB"
FT                   /id="PRO_0000220495"
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:11311241"
FT   MUTAGEN         525
FT                   /note="K->A: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:11311241"
FT   MUTAGEN         528
FT                   /note="K->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11311241"
FT   CONFLICT        244
FT                   /note="C -> FD (in Ref. 1; AAC46234)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="V -> VV (in Ref. 1; AAC46234)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="R -> G (in Ref. 1; AAC46234)"
FT                   /evidence="ECO:0000305"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   HELIX           73..90
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   HELIX           96..107
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   HELIX           118..142
FT                   /evidence="ECO:0007829|PDB:4DID"
FT   HELIX           147..166
FT                   /evidence="ECO:0007829|PDB:4DID"
SQ   SEQUENCE   561 AA;  61935 MW;  A484B55502CFA643 CRC64;
     MQIQSFYHSA SLKTQEAFKS LQKTLYNGMQ ILSGQGKAPA KAPDARPEII VLREPGATWG
     NYLQHQKASN HSLHNLYNLQ RDLLTVAATV LGKQDPVLTS MANQMELAKV KADRPATKQE
     EAAAKALKKN LIELIAARTQ QQDGLPAKEA HRFAAVAFRD AQVKQLNNQP WQTIKNTLTH
     NGHHYTNTQL PAAEMKIGAK DIFPSAYEGK GVCSWDTKNI HHANNLWMST VSVHEDGKDK
     TLFCGIRHGV LSPYHEKDPL LRHVGAENKA KEVLTAALFS KPELLNKALA GEAVSLKLVS
     VGLLTASNIF GKEGTMVEDQ MRAWQSLTQP GKMIHLKIRN KDGDLQTVKI KPDVAAFNVG
     VNELALKLGF GLKASDSYNA EALHQLLGND LRPEARPGGW VGEWLAQYPD NYEVVNTLAR
     QIKDIWKNNQ HHKDGGEPYK LAQRLAMLAH EIDAVPAWNC KSGKDRTGMM DSEIKREIIS
     LHQTHMLSAP GSLPDSGGQK IFQKVLLNSG NLEIQKQNTG GAGNKVMKNL SPEVLNLSYQ
     KRVGDENIWQ SVKGISSLIT S
 
 
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