GRPE_VIBHA
ID GRPE_VIBHA Reviewed; 198 AA.
AC Q6IT00;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
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 Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9747709; DOI=10.1007/s004380050803;
RA Klein G., Zmijewski M., Krzewska J., Czeczatka M., Lipinska B.;
RT "Cloning and characterization of the dnaK heat shock operon of the marine
RT bacterium Vibrio harveyi.";
RL Mol. Gen. Genet. 259:179-189(1998).
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; AY639008; AAT39534.1; -; Genomic_DNA.
DR RefSeq; WP_005447652.1; NZ_UAVF01000034.1.
DR AlphaFoldDB; Q6IT00; -.
DR SMR; Q6IT00; -.
DR STRING; 669.AL538_12720; -.
DR GeneID; 57820336; -.
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..198
FT /note="Protein GrpE"
FT /id="PRO_0000113892"
SQ SEQUENCE 198 AA; 22308 MW; F43306E2C5C26C05 CRC64;
MSNEENKVTE EELDQIIEEA EKVEAAAQEA EAELEEIGDE KDAKIAQLEA ALLSSETKVK
DQQDAVLRSK AEVENMRRRT EQEIDKARKY ALNKFAEELL PVIDNLERAI QAADAEHEVV
KPILEGVELT HKTFVDAVSK FGLKEINPEG EAFNPEFHQA MSIQESPDHE SNTVMFVMQK
GYELNGRVVR PAMVMVAK