ID   SOPE2_SALPA             Reviewed;         240 AA.
AC   Q5PHN0;
DT   29-MAR-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 sopE2;
DE   AltName: Full=Effector protein sopE2;
DE   AltName: Full=Toxin sopE2;
GN   Name=sopE2; OrderedLocusNames=SPA1018;
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 CDC42 by directly engaging this Rho GTPase and
CC       acting as potent guanine nucleotide exchange factor (GEF). This
CC       activation results in actin cytoskeleton rearrangements and stimulates
CC       membrane ruffling, promoting bacterial entry into non-phagocytic cells.
CC       Chaperone InvB is required for secretion, translocation and
CC       stabilization of intracellular levels of sopE2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted via the
CC       type III secretion system 1 (SPI-1 TTSS). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GEF (guanine exchange factor) SopE family.
CC       {ECO:0000305}.
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DR   EMBL; CP000026; AAV76990.1; -; Genomic_DNA.
DR   RefSeq; WP_001284212.1; NC_006511.1.
DR   AlphaFoldDB; Q5PHN0; -.
DR   BMRB; Q5PHN0; -.
DR   SMR; Q5PHN0; -.
DR   EnsemblBacteria; AAV76990; AAV76990; SPA1018.
DR   KEGG; spt:SPA1018; -.
DR   HOGENOM; CLU_107159_0_0_6; -.
DR   OMA; LDIKSHA; -.
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 sopE2"
FT                   /id="PRO_0000220741"
FT   REGION          78..240
FT                   /note="GEF catalytic domain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  26359 MW;  57E10A65695BB756 CRC64;
     MANITLSTQH YRIHRSDVEP VKEKTTDKDV FAKSITAVRN SFISLSTSLS DRFSLHLQTD
     IPTTHFHRGS ASEGRAVLTS KTVKDFMLQK LNSLDIKGNA SKDPAYARQT CEAMLSAVYS
     NNKDHCCKLL ISKGVSITPF LKEIGEAAQN AGLPGEIKNG VFTPGGAGAN PFVVPLIAAA
     SIKYPHMFIN HNQQVSFKAY AEKIVMKEVT PLFNKGTMPT PQQFQLTIEN IANKYLQNAS