ID A2WCG2_9BURK Unreviewed; 181 AA.
AC A2WCG2; A0A0D5J4V8;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU000639};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151};
GN ORFNames=BDAG_02421 {ECO:0000313|EMBL:EAY69658.1};
OS Burkholderia dolosa AU0158.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY69658.1, ECO:0000313|Proteomes:UP000053482};
RN [1] {ECO:0000313|Proteomes:UP000053482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU0158 {ECO:0000313|Proteomes:UP000053482};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA Alvarado L., Lory S., LiPuma J.;
RT "The Genome Sequence of Burkholderia dolosa (strain AU0158).";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC heat shock by preventing the aggregation of stress-denatured proteins,
CC in association with DnaK and GrpE. It is the nucleotide exchange factor
CC for DnaK and may function as a thermosensor. Unfolded proteins bind
CC initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK
CC hydrolyzes its bound ATP, resulting in the formation of a stable
CC complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the
CC release of the substrate protein, thus completing the reaction cycle.
CC Several rounds of ATP-dependent interactions between DnaJ, DnaK and
CC GrpE are required for fully efficient folding. {ECO:0000256|HAMAP-
CC Rule:MF_01151, ECO:0000256|RuleBase:RU000639}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU004478}.
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DR EMBL; CH482380; EAY69658.1; -; Genomic_DNA.
DR RefSeq; WP_006765100.1; NZ_CP009795.1.
DR AlphaFoldDB; A2WCG2; -.
DR GeneID; 64462116; -.
DR PATRIC; fig|350701.8.peg.2607; -.
DR HOGENOM; CLU_057217_6_1_4; -.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000053482; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 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; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01151};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
SQ SEQUENCE 181 AA; 19399 MW; E4BD5B749933D1AF CRC64;
MENTQENPAT PSAEDIGSDK QAEQGAAPAA EAADAALAEA QAKVAELQES YLRAKAETEN
VRRRAQEDVA KAHKFAIESF AEHLLPVLDS LEAAVGDTSG DIAKVREGVE LTLRQLTSAL
EKGRVVAINP VGEKFDPHQH QAISMVPAEQ EPNTVVTVLQ KGYMIADRVL RPALVTVAQP
K
//