ID   SOPE_SALPA              Reviewed;         240 AA.
AC   Q5PFI5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Guanine nucleotide exchange factor SopE;
DE   AltName: Full=Effector protein SopE;
DE   AltName: Full=Toxin SopE;
GN   Name=sopE; OrderedLocusNames=SPA2564;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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. Note=Secreted via the type III
CC       secretion system 1 (SPI-1 TTSS).
CC   -!- SIMILARITY: Belongs to the GEF (guanine exchange factor) SopE family.
CC       {ECO:0000305}.
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DR   EMBL; CP000026; AAV78431.1; -; Genomic_DNA.
DR   RefSeq; WP_000161709.1; NC_006511.1.
DR   AlphaFoldDB; Q5PFI5; -.
DR   SMR; Q5PFI5; -.
DR   EnsemblBacteria; AAV78431; AAV78431; SPA2564.
DR   KEGG; spt:SPA2564; -.
DR   HOGENOM; CLU_107159_0_0_6; -.
DR   OMA; YATIYSE; -.
DR   Proteomes; UP000008185; Chromosome.
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_0000220738"
FT   REGION          78..240
FT                   /note="GEF catalytic domain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  26713 MW;  F6208EC246669B64 CRC64;
     MTKITLSPQN FRIQKQETTL LKEKSTEKNS LAKSILAVKN HFIELRSKLS ERFISHKNTE
     SSATHFHRGS ASEGRAVLTN KVVKDFMLQT LNDIDIRGSA SKDPAYASQT REAILSAVYS
     KNKDQCCNLL ISKGINIAPF LQEIGEAAKN VGLPGTTKND VFTPSGAGAN PFITPLISSA
     NSKYPRMFIN QHQQASFKIY AEKIIMTEVA PLFNECAMPT PQQFQLILEN IANKYIQYTP