(data stored in ACNUC7421 zone)

SWISSPROT: GRPE_PARXL

ID   GRPE_PARXL              Reviewed;         194 AA.
AC   Q145F3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151};
DE   AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151};
GN   Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151};
GN   OrderedLocusNames=Bxeno_A0498; ORFNames=Bxe_A3963;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic
CC       and heat shock by preventing the aggregation of stress-denatured
CC       proteins, in association with DnaK and GrpE. It is the nucleotide
CC       exchange factor for DnaK and may function as a thermosensor.
CC       Unfolded proteins bind initially to DnaJ; upon interaction with
CC       the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC       in the formation of a stable complex. GrpE releases ADP from DnaK;
CC       ATP binding to DnaK triggers the release of the substrate protein,
CC       thus completing the reaction cycle. Several rounds of ATP-
CC       dependent interactions between DnaJ, DnaK and GrpE are required
CC       for fully efficient folding. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01151}.
DR   EMBL; CP000270; ABE29036.1; -; Genomic_DNA.
DR   RefSeq; WP_007179202.1; NZ_CP008760.1.
DR   SMR; Q145F3; -.
DR   STRING; 266265.Bxe_A3963; -.
DR   EnsemblBacteria; ABE29036; ABE29036; Bxe_A3963.
DR   GeneID; 4002267; -.
DR   KEGG; bxb:DR64_1639; -.
DR   KEGG; bxe:Bxe_A3963; -.
DR   eggNOG; ENOG4105K90; Bacteria.
DR   eggNOG; COG0576; LUCA.
DR   HOGENOM; HOG000252083; -.
DR   KO; K03687; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 1906715at2; -.
DR   BioCyc; BXEN266265:BXE_RS02495-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00446; GrpE; 1.
DR   Gene3D; 2.30.22.10; -; 1.
DR   Gene3D; 3.90.20.20; -; 1.
DR   HAMAP; MF_01151; GrpE; 1.
DR   InterPro; IPR000740; GrpE.
DR   InterPro; IPR013805; GrpE_coiled_coil.
DR   InterPro; IPR009012; GrpE_head.
DR   PANTHER; PTHR21237; PTHR21237; 1.
DR   Pfam; PF01025; GrpE; 1.
DR   PRINTS; PR00773; GRPEPROTEIN.
DR   SUPFAM; SSF51064; SSF51064; 1.
DR   SUPFAM; SSF58014; SSF58014; 1.
DR   PROSITE; PS01071; GRPE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145F3.
DR   SWISS-2DPAGE; Q145F3.
KW   Chaperone; Complete proteome; Cytoplasm; Reference proteome;
KW   Stress response.
FT   CHAIN         1    194       Protein GrpE.
FT                                /FTId=PRO_1000053562.
SQ   SEQUENCE   194 AA;  20718 MW;  C8E7464859B460FC CRC64;
     MENTQENPTS QNPKPAEETA RQAAEAAAPQ QEAAANAATD SPASAEQAAL AEAQAKIAEL
     QESFLRAKAE TENVRRRAQE DVAKAHKFAI ESFAEHLLPV IDSLEAAVAH SSDDPAKVRE
     GVELTLRQLT GALEKGRVVA LNPVGEKFDP HRHQAISMVP ADQEPNTVVA VLQKGFVIAD
     RVLRPALVTV AAPK
//

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