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SOPE2_SALTY
ID   SOPE2_SALTY             Reviewed;         240 AA.
AC   Q7CQD4; Q9KIZ2; Q9L8K7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Guanine nucleotide exchange factor sopE2;
DE   AltName: Full=Effector protein sopE2;
DE   AltName: Full=Toxin sopE2;
GN   Name=sopE2; OrderedLocusNames=STM1855;
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], AND PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=F98;
RX   PubMed=10735884; DOI=10.1128/jb.182.8.2341-2344.2000;
RA   Bakshi C.S., Singh V.P., Wood M.W., Jones P.W., Wallis T.S., Galyov E.E.;
RT   "Identification of SopE2, a Salmonella secreted protein which is highly
RT   homologous to SopE and involved in bacterial invasion of epithelial
RT   cells.";
RL   J. Bacteriol. 182:2341-2344(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=SL1344;
RX   PubMed=10931274; DOI=10.1046/j.1365-2958.2000.01933.x;
RA   Stender S., Friebel A., Linder S., Rohde M., Mirold S., Hardt W.-D.;
RT   "Identification of SopE2 from Salmonella typhimurium, a conserved guanine
RT   nucleotide exchange factor for Cdc42 of the host cell.";
RL   Mol. Microbiol. 36:1206-1221(2000).
RN   [3]
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   [4]
RP   INTERACTION WITH CHAPERONE INVB.
RC   STRAIN=SL1344;
RX   PubMed=14617659; DOI=10.1128/jb.185.23.6950-6967.2003;
RA   Ehrbar K., Friebel A., Miller S.I., Hardt W.-D.;
RT   "Role of the Salmonella pathogenicity island 1 (SPI-1) protein InvB in type
RT   III secretion of SopE and SopE2, two Salmonella effector proteins encoded
RT   outside of SPI-1.";
RL   J. Bacteriol. 185:6950-6967(2003).
RN   [5]
RP   FUNCTION.
RC   STRAIN=F98;
RX   PubMed=15321998; DOI=10.1128/iai.72.9.5052-5062.2004;
RA   Huang F.-C., Werne A., Li Q., Galyov E.E., Walker W.A., Cherayil B.J.;
RT   "Cooperative interactions between flagellin and SopE2 in the epithelial
RT   interleukin-8 response to Salmonella enterica serovar typhimurium
RT   infection.";
RL   Infect. Immun. 72:5052-5062(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       Also activates NF-kB, p38 and ERK kinases, which are known to be
CC       involved in the induction of IL-8 expression. Chaperone InvB is
CC       required for secretion, translocation and stabilization of
CC       intracellular levels of sopE2. {ECO:0000269|PubMed:10931274,
CC       ECO:0000269|PubMed:15321998}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via the type III
CC       secretion system 1 (SPI-1 TTSS).
CC   -!- MISCELLANEOUS: SopE2 is highly conserved among Salmonella isolates of
CC       the SARA collection.
CC   -!- SIMILARITY: Belongs to the GEF (guanine exchange factor) SopE family.
CC       {ECO:0000305}.
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DR   EMBL; AF200952; AAF63159.1; -; Genomic_DNA.
DR   EMBL; AF217274; AAF91225.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20770.1; -; Genomic_DNA.
DR   RefSeq; NP_460811.1; NC_003197.2.
DR   RefSeq; WP_000182072.1; NC_003197.2.
DR   PDB; 1R6E; NMR; -; A=73-240.
DR   PDB; 1R9K; NMR; -; A=69-240.
DR   PDBsum; 1R6E; -.
DR   PDBsum; 1R9K; -.
DR   AlphaFoldDB; Q7CQD4; -.
DR   BMRB; Q7CQD4; -.
DR   SMR; Q7CQD4; -.
DR   IntAct; Q7CQD4; 1.
DR   STRING; 99287.STM1855; -.
DR   PaxDb; Q7CQD4; -.
DR   EnsemblBacteria; AAL20770; AAL20770; STM1855.
DR   GeneID; 1253374; -.
DR   KEGG; stm:STM1855; -.
DR   PATRIC; fig|99287.12.peg.1960; -.
DR   HOGENOM; CLU_107159_0_0_6; -.
DR   OMA; LDIKSHA; -.
DR   BioCyc; SENT99287:STM1855-MON; -.
DR   EvolutionaryTrace; Q7CQD4; -.
DR   PHI-base; PHI:6800; -.
DR   PHI-base; PHI:7921; -.
DR   Proteomes; UP000001014; 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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; GTPase activation;
KW   Guanine-nucleotide releasing factor; Reference proteome; Secreted;
KW   Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10735884"
FT   CHAIN           2..240
FT                   /note="Guanine nucleotide exchange factor sopE2"
FT                   /id="PRO_0000220742"
FT   REGION          78..240
FT                   /note="GEF catalytic domain"
FT                   /evidence="ECO:0000250"
FT   VARIANT         125
FT                   /note="Q -> H (in strain: F98)"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           83..94
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           96..102
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           104..133
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           137..150
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           173..183
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           185..188
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           191..209
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           210..213
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:1R6E"
FT   HELIX           221..237
FT                   /evidence="ECO:0007829|PDB:1R6E"
SQ   SEQUENCE   240 AA;  26448 MW;  B4A113292FABD65F CRC64;
     MTNITLSTQH YRIHRSDVEP VKEKTTEKDI FAKSITAVRN SFISLSTSLS DRFSLHQQTD
     IPTTHFHRGN ASEGRAVLTS KTVKDFMLQK LNSLDIKGNA SKDPAYARQT CEAILSAVYS
     NNKDQCCKLL ISKGVSITPF LKEIGEAAQN AGLPGEIKNG VFTPGGAGAN PFVVPLIASA
     SIKYPHMFIN HNQQVSFKAY AEKIVMKEVT PLFNKGTMPT PQQFQLTIEN IANKYLQNAS
 
 
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