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 19-JAN-2010, entry version 49. DE RecName: Full=Protein grpE; DE AltName: Full=HSP-70 cofactor; GN Name=grpE; OrderedLocusNames=SO_1524; OS Shewanella oneidensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=70863; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1; RX MEDLINE=22297686; 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., RA Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., RA Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., RA White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., RA Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., RA 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 CC and heat shock by preventing the aggregation of stress-denatured CC proteins, in association with dnaK and grpE. It is the nucleotide CC exchange factor for dnaK and may function as a thermosensor. CC Unfolded proteins bind initially to dnaJ; upon interaction with CC the dnaJ-bound protein, dnaK hydrolyzes its bound ATP, resulting CC in the formation of a stable complex. GrpE releases ADP from dnaK; CC ATP binding to dnaK triggers the release of the substrate protein, CC thus completing the reaction cycle. Several rounds of ATP- CC dependent interactions between dnaJ, dnaK and grpE are required CC for fully efficient folding (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- SIMILARITY: Belongs to the grpE family. 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; -. DR SMR; Q8EGS0; 35-194. DR GeneID; 1169333; -. DR GenomeReviews; AE014299_GR; SO_1524. DR KEGG; son:SO_1524; -. DR NMPDR; fig|211586.1.peg.1412; -. DR TIGR; SO_1524; -. DR HOGENOM; HBG732630; -. DR OMA; NLHQAVM; -. DR BioCyc; SONE211586:SO_1524-MONOMER; -. DR GO; GO:0005739; C:mitochondrion; IEA:InterPro. 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 GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:InterPro. DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. DR HAMAP; MF_01151; GrpE; 1; -. DR InterPro; IPR000740; GrpE. DR InterPro; IPR013805; GrpE_coiled_coil. DR InterPro; IPR009012; GrpE_head. DR Gene3D; G3DSA:3.90.20.20; GrpE_coiled_coil; 1. DR Gene3D; G3DSA:2.30.22.10; GrpE_head; 1. DR PANTHER; PTHR21237; GrpE; 1. DR Pfam; PF01025; GrpE; 1. DR PRINTS; PR00773; GRPEPROTEIN. DR PROSITE; PS01071; GRPE; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Stress response. FT CHAIN 1 206 Protein grpE. FT /FTId=PRO_0000113852. 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 //