BOPE_BURPS
ID BOPE_BURPS Reviewed; 261 AA.
AC Q63K41;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Guanine nucleotide exchange factor BopE;
DE AltName: Full=Effector protein BopE;
GN Name=bopE; OrderedLocusNames=BPSS1525;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [2]
RP ROLE IN INVASION OF HOST CELLS.
RC STRAIN=10276;
RX PubMed=12410823; DOI=10.1046/j.1365-2958.2002.03190.x;
RA Stevens M.P., Wood M.W., Taylor L.A., Monaghan P., Hawes P., Jones P.W.,
RA Wallis T.S., Galyov E.E.;
RT "An Inv/Mxi-Spa-like type III protein secretion system in Burkholderia
RT pseudomallei modulates intracellular behaviour of the pathogen.";
RL Mol. Microbiol. 46:649-659(2002).
RN [3]
RP ROLE IN INVASION OF HOST CELLS, AND SUBCELLULAR LOCATION.
RC STRAIN=576;
RX PubMed=12897019; DOI=10.1128/jb.185.16.4992-4996.2003;
RA Stevens M.P., Friebel A., Taylor L.A., Wood M.W., Brown P.J., Hardt W.-D.,
RA Galyov E.E.;
RT "A Burkholderia pseudomallei type III secreted protein, BopE, facilitates
RT bacterial invasion of epithelial cells and exhibits guanine nucleotide
RT exchange factor activity.";
RL J. Bacteriol. 185:4992-4996(2003).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=576;
RX PubMed=15063321; DOI=10.1016/j.bbapap.2003.11.004;
RA Upadhyay A., Williams C., Gill A.C., Philippe D.L., Davis K., Taylor L.A.,
RA Stevens M.P., Galyov E.E., Bagby S.;
RT "Biophysical characterization of the catalytic domain of guanine nucleotide
RT exchange factor BopE from Burkholderia pseudomallei.";
RL Biochim. Biophys. Acta 1698:111-119(2004).
RN [5]
RP ROLE IN VIRULENCE.
RC STRAIN=576;
RX PubMed=15289563; DOI=10.1099/mic.0.27146-0;
RA Stevens M.P., Haque A., Atkins T., Hill J., Wood M.W., Easton A.,
RA Nelson M., Underwood-Fowler C., Titball R.W., Bancroft G.J., Galyov E.E.;
RT "Attenuated virulence and protective efficacy of a Burkholderia
RT pseudomallei bsa type III secretion mutant in murine models of
RT melioidosis.";
RL Microbiology 150:2669-2676(2004).
RN [6]
RP IMMUNOGENICITY.
RC STRAIN=576;
RX PubMed=17041850; DOI=10.1086/508217;
RA Haque A., Chu K., Easton A., Stevens M.P., Galyov E.E., Atkins T.,
RA Titball R., Bancroft G.J.;
RT "A live experimental vaccine against Burkholderia pseudomallei elicits CD4+
RT T cell-mediated immunity, priming T cells specific for 2 type III secretion
RT system proteins.";
RL J. Infect. Dis. 194:1241-1248(2006).
RN [7]
RP STRUCTURE BY NMR OF 78-261, MUTAGENESIS OF ARG-207; ASN-216; ASN-224 AND
RP ARG-230, AND INTERACTION WITH HUMAN CDC42.
RX PubMed=18052936; DOI=10.1042/bj20071546;
RA Upadhyay A., Wu H.-L., Williams C., Field T., Galyov E.E.,
RA van den Elsen J.M.H., Bagby S.;
RT "The guanine-nucleotide-exchange factor BopE from Burkholderia pseudomallei
RT adopts a compact version of the Salmonella SopE/SopE2 fold and undergoes a
RT closed-to-open conformational change upon interaction with Cdc42.";
RL Biochem. J. 411:485-493(2008).
CC -!- FUNCTION: Activator for both CDC42 and RAC1 by directly interacting
CC with these Rho GTPases and acting as a guanine nucleotide exchange
CC factor (GEF). This activation results in actin cytoskeleton
CC rearrangements and stimulates membrane ruffling, thus promoting
CC bacterial entry into non-phagocytic cells.
CC {ECO:0000269|PubMed:12410823, ECO:0000269|PubMed:12897019,
CC ECO:0000269|PubMed:15289563}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active in pH ranges of 3.5-10.5. {ECO:0000269|PubMed:15063321};
CC -!- SUBUNIT: Monomer (Probable). Interacts with human CDC42.
CC {ECO:0000269|PubMed:15063321, ECO:0000269|PubMed:18052936,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12897019}.
CC Note=Secreted via the bsa type III secretion system. {ECO:0000250}.
CC -!- MISCELLANEOUS: Immunogenic protein that elicits T-cell-mediated
CC immunity in mice.
CC -!- SIMILARITY: Belongs to the GEF (guanine exchange factor) SopE family.
CC {ECO:0000305}.
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DR EMBL; BX571966; CAH38998.1; -; Genomic_DNA.
DR RefSeq; WP_004528812.1; NZ_CP009537.1.
DR RefSeq; YP_111531.1; NC_006351.1.
DR PDB; 2JOK; NMR; -; A=78-261.
DR PDB; 2JOL; NMR; -; A=78-261.
DR PDBsum; 2JOK; -.
DR PDBsum; 2JOL; -.
DR AlphaFoldDB; Q63K41; -.
DR SMR; Q63K41; -.
DR STRING; 272560.BPSS1525; -.
DR EnsemblBacteria; CAH38998; CAH38998; BPSS1525.
DR KEGG; bps:BPSS1525; -.
DR PATRIC; fig|272560.51.peg.4880; -.
DR eggNOG; ENOG5033HJR; Bacteria.
DR OMA; RQAIRHF; -.
DR EvolutionaryTrace; Q63K41; -.
DR Proteomes; UP000000605; Chromosome 2.
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 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; GTPase activation; Guanine-nucleotide releasing factor;
KW Reference proteome; Secreted; Virulence.
FT CHAIN 1..261
FT /note="Guanine nucleotide exchange factor BopE"
FT /id="PRO_0000344030"
FT MUTAGEN 207
FT /note="R->E: Loss of GEF activity; when associated with P-
FT 216."
FT /evidence="ECO:0000269|PubMed:18052936"
FT MUTAGEN 216
FT /note="N->P: Loss of GEF activity; when associated with E-
FT 207."
FT /evidence="ECO:0000269|PubMed:18052936"
FT MUTAGEN 224
FT /note="N->P: Increased GEF activity; when associated with
FT Q-230."
FT /evidence="ECO:0000269|PubMed:18052936"
FT MUTAGEN 230
FT /note="R->Q: Increased GEF activity; when associated with
FT P-224."
FT /evidence="ECO:0000269|PubMed:18052936"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 84..99
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:2JOK"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:2JOL"
FT HELIX 110..132
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2JOK"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:2JOK"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2JOK"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:2JOK"
FT HELIX 221..251
FT /evidence="ECO:0007829|PDB:2JOK"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2JOK"
SQ SEQUENCE 261 AA; 28705 MW; A44EB3AB9CBFA621 CRC64;
MTYNPRIGGF THVKQASFDV HVKRGEAQPR TSFAQQIKRI FSKIGETLGQ LFRHRAPDSA
PGRVRLQGVR YVGSYRPTGD AKQAIRHFVD EAVKQVAHAR TPEIRQDAEF GRQVYEATLC
AIFSEAKDRF CMDPATRAGN VRPAFIEALG DAARATGLPG ADKQGVFTPS GAGTNPLYTE
IRLRADTLMG AELAARPEYR ELQPYARQQA IDLVANALPA ERSNTLVEFR QTVQTLEATY
RRAAQDASRD EKGATNAADG A
