GRPE_DICNV
ID GRPE_DICNV Reviewed; 187 AA.
AC A5EYG2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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}; OrderedLocusNames=DNO_0825;
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A;
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
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:0000255|HAMAP-
CC 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}.
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DR EMBL; CP000513; ABQ14243.1; -; Genomic_DNA.
DR RefSeq; WP_012031148.1; NC_009446.1.
DR AlphaFoldDB; A5EYG2; -.
DR SMR; A5EYG2; -.
DR STRING; 246195.DNO_0825; -.
DR EnsemblBacteria; ABQ14243; ABQ14243; DNO_0825.
DR KEGG; dno:DNO_0825; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_0_6; -.
DR OMA; YAYEKIA; -.
DR OrthoDB; 1906715at2; -.
DR Proteomes; UP000000248; Chromosome.
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;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..187
FT /note="Protein GrpE"
FT /id="PRO_1000053574"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 187 AA; 21266 MW; E488DB202ED0594F CRC64;
MHDPKESLET NIQETESQEK LPETPIIEEE PILTLPDDQI NQLQQEVAEL KDQLIWQKAE
NENLRKRQAR ELENAYKFAS ERLLKDLLPV IDSLNLGLQA ALDTENEAVK QFITGSEMTL
TMFQETLARH GIEEINPVGE KFNPELHEAV TMTPSEAHEP NTVIQVTQKG YLLNGRTVRA
AQVIVSK