GRPE_WIGBR
ID GRPE_WIGBR Reviewed; 218 AA.
AC Q8D392;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 89.
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=WIGBR1090;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC24255.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000021; BAC24255.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_050702910.1; NC_004344.2.
DR AlphaFoldDB; Q8D392; -.
DR SMR; Q8D392; -.
DR STRING; 36870.25166064; -.
DR PRIDE; Q8D392; -.
DR EnsemblBacteria; BAC24255; BAC24255; BAC24255.
DR KEGG; wbr:grpE; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_0_6; -.
DR OMA; YAYEKIA; -.
DR OrthoDB; 1906715at2; -.
DR Proteomes; UP000000562; 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..218
FT /note="Protein GrpE"
FT /id="PRO_0000113897"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 25532 MW; CFC57A8412BE5B03 CRC64;
MKEKNSNKIN EDKLNKKSEV KNKKEEEIIN NKKQTTEKKI NLNKNNISDE IIPEKINFND
QKNIIENLKK NLSKEKKSKH DLILRNQAEM ENLMKRTQAN IEKSYKFALE KFSIALLPII
DNLERTKNLL EKENEKNKNI NPIEEGINLT LKEFIKVIHS FGIKEIDKKN IPFDPKIHEA
MTVIDDKNKK TNQVVEIMQK GYILNGRLLR PAMVVVSK
