ID   SOPE_SALDU              Reviewed;         240 AA.
AC   O06949;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Guanine nucleotide exchange factor SopE;
DE   AltName: Full=Effector protein SopE;
DE   AltName: Full=Toxin SopE;
GN   Name=sopE;
OS   Salmonella dublin.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=98360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16; 40-44 AND
RP   184-194.
RC   STRAIN=2229;
RX   PubMed=8930917; DOI=10.1046/j.1365-2958.1996.00116.x;
RA   Wood M.W., Rosqvist R., Mullan P.B., Edwards M.H., Galyov E.E.;
RT   "SopE, a secreted protein of Salmonella dublin, is translocated into the
RT   target eukaryotic cell via a sip-dependent mechanism and promotes bacterial
RT   entry.";
RL   Mol. Microbiol. 22:327-338(1996).
RN   [2]
RP   PROPHAGE-RELATED REGION.
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: Acts in concert with other proteins to mediate cellular
CC       responses leading to bacterial internalization. Activator for both
CC       CDC42 and RAC1 by directly engaging these Rho GTPases and acting as
CC       potent guanine nucleotide exchange factor (GEF). This activation
CC       results in actin cytoskeleton rearrangements and stimulates membrane
CC       ruffling, promoting bacterial entry into non-phagocytic cells (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via the type III
CC       secretion system 1 (SPI-1 TTSS).
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; L78932; AAB51429.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06949; -.
DR   SMR; O06949; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; GTPase activation;
KW   Guanine-nucleotide releasing factor; Secreted; Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8930917"
FT   CHAIN           2..240
FT                   /note="Guanine nucleotide exchange factor SopE"
FT                   /id="PRO_0000220732"
FT   REGION          78..240
FT                   /note="GEF catalytic domain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  26738 MW;  CD951FCAA87930E3 CRC64;
     MTKITLFPHN FRIQKQEATP LKEKSTEKNS LAKSILAVKN HFIKLNSKLS ERFISHKNTE
     SSATHFHRGS ASEGRAVLTN KVVKNFMLQT LHDIDIRGSA SKDPAYASQT REAILSAVYS
     KYKDQYCNLL ISKGIDIAPF LKEIGEAAQN AGLPGATKND VFSPSGAGAN PFITPLITSA
     YSKYPHMFTS QHQKASFNIY AEKIIMTEVV PLFNECAMPT PQQFQQILEN IANKYIQNTP