ID GRPE_SHEON Reviewed; 206 AA. AC Q8EGS0; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-DEC-2022, entry version 102. 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=SO_1524; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014299; AAN54585.1; -; Genomic_DNA. DR RefSeq; NP_717141.1; NC_004347.2. DR RefSeq; WP_011071703.1; NZ_CP053946.1. DR AlphaFoldDB; Q8EGS0; -. DR SMR; Q8EGS0; -. DR STRING; 211586.SO_1524; -. DR PaxDb; Q8EGS0; -. DR KEGG; son:SO_1524; -. DR PATRIC; fig|1028802.3.peg.931; -. DR eggNOG; COG0576; Bacteria. DR HOGENOM; CLU_057217_6_0_6; -. DR OMA; YAYEKIA; -. DR OrthoDB; 1906715at2; -. DR PhylomeDB; Q8EGS0; -. DR BioCyc; SONE211586:G1GMP-1408-MON; -. DR Proteomes; UP000008186; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central. DR GO; GO:0051087; F:chaperone binding; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. 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; GRPE PROTEIN; 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; Cytoplasm; Reference proteome; Stress response. FT CHAIN 1..206 FT /note="Protein GrpE" FT /id="PRO_0000113852" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 206 AA; 22703 MW; 2F1C6A29FE7C42A7 CRC64; MSNESIKAEQ DLIHEGVESE VSTEEASLID ELTQANFRIE ELEQLLADAL AKVDEQKDSV IRAAAEVDNI RRRAAMDVEK ANKFALEKFA NELLPVLDNM ERALQGTNPQ DETTKAIYEG VELTQKSLLT AVAKFGVKQI DPQGQAFNPD QHQAIGMQPS AEFPTNTVML VMQKGYELNS RLLRPAMVMV SQGGPSQESA SIDIEA //