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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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