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SOPE_SALGL
ID   SOPE_SALGL              Reviewed;         240 AA.
AC   Q8VSQ6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Guanine nucleotide exchange factor SopE;
DE   AltName: Full=Effector protein SopE;
DE   AltName: Full=Toxin SopE;
GN   Name=sopE;
OS   Salmonella gallinarum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROPHAGE-RELATED REGION.
RC   STRAIN=X3796;
RX   PubMed=11545581; DOI=10.1006/jmbi.2001.4950;
RA   Mirold S., Rabsch W., Tschaepe H., Hardt W.-D.;
RT   "Transfer of the Salmonella type III effector sopE between unrelated phage
RT   families.";
RL   J. Mol. Biol. 312:7-16(2001).
CC   -!- FUNCTION: Activator for both CDC42 and RAC1 by directly engaging these
CC       Rho GTPases and acting as potent guanine nucleotide exchange factor
CC       (GEF). This activation results in actin cytoskeleton rearrangements and
CC       stimulates membrane ruffling, promoting bacterial entry into non-
CC       phagocytic cells (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   -!- MISCELLANEOUS: Encoded within a lambda-like prophage region with
CC       similarity to GIFSY phages.
CC   -!- SIMILARITY: Belongs to the GEF (guanine exchange factor) SopE family.
CC       {ECO:0000305}.
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DR   EMBL; AF380340; AAL67197.1; -; Genomic_DNA.
DR   RefSeq; WP_000161702.1; NZ_RHEL01000001.1.
DR   AlphaFoldDB; Q8VSQ6; -.
DR   SMR; Q8VSQ6; -.
DR   PATRIC; fig|594.9.peg.2805; -.
DR   OMA; YATIYSE; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:InterPro.
DR   GO; GO:0090630; P:activation of GTPase activity; IEA:InterPro.
DR   Gene3D; 1.10.4120.10; -; 1.
DR   InterPro; IPR005414; SopE.
DR   InterPro; IPR035949; SopE-like_GEF_dom_sf.
DR   InterPro; IPR016019; SopE_GEF_dom.
DR   InterPro; IPR016018; SopE_N_dom.
DR   Pfam; PF05364; SecIII_SopE_N; 1.
DR   Pfam; PF07487; SopE_GEF; 1.
DR   PIRSF; PIRSF034781; SecIII_sopE; 1.
DR   PRINTS; PR01593; SOPEPROTEIN.
DR   SUPFAM; SSF81832; SSF81832; 1.
PE   3: Inferred from homology;
KW   GTPase activation; Guanine-nucleotide releasing factor; Secreted;
KW   Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..240
FT                   /note="Guanine nucleotide exchange factor SopE"
FT                   /id="PRO_0000220735"
FT   REGION          78..240
FT                   /note="GEF catalytic domain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  26751 MW;  388DE85164D82210 CRC64;
     MTKITLFPHN FRIQKQETTP LKEKSTEKNS LAKSILAVKN HFIKLNSKLS ERFISHKNTE
     SSATHFHRGS ASEGRAVLTN KVVKNFMLQT LHDIDIRGSA SKDPAYASQT REAILSAVYS
     KYKDQYCNLL ISKGIDIAPF LKEIGEAAQN AGLPGATKND VFTPSGAGAN PFITPLITSA
     YSKYPHMFTS QHQKASFNIY AEKIIMTEVV PLFNECAMPT PQQFQQILEN IANKYIPNTP
 
 
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