GRPE_FUSNP
ID GRPE_FUSNP Reviewed; 202 AA.
AC Q70WY9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 68.
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};
OS Fusobacterium nucleatum subsp. polymorphum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=76857;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10953 / DSM 20482 / CCUG 9126 / JCM 12990 / NCTC 10562 / 555A;
RA Skar C.K., Villoing S.C., Bakken V.;
RL Submitted (OCT-2002) 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: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; AJ512795; CAD55135.1; -; Genomic_DNA.
DR RefSeq; WP_005897684.1; NZ_NIRO01000008.1.
DR AlphaFoldDB; Q70WY9; -.
DR SMR; Q70WY9; -.
DR STRING; 76857.RO02_09555; -.
DR GeneID; 45634023; -.
DR GeneID; 60658619; -.
DR PATRIC; fig|76857.9.peg.193; -.
DR OrthoDB; 1906715at2; -.
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; Stress response.
FT CHAIN 1..202
FT /note="Protein GrpE"
FT /id="PRO_0000113789"
FT REGION 21..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 23507 MW; 120F418469E1913E CRC64;
MKDKDIKEEV LKEEINKEVN EELKNEEVKE ETHEHEHKHG GHTCCGKHGH KHNDEEIGKL
KAEIEEWKNE YLRKQADFQN FTKRKEKEVD ELKKFASEKI ITQFLGSLDN LERAIESSIE
SKDFDSLLKG IEMIVRNLKD IMSAEGVEEI KTEGVYDPVY HHAVGVEANE DFKEDEIVKV
LQKGYMMKGK VIRPAMVIVC KK
