GRPE_SINMW
ID GRPE_SINMW Reviewed; 208 AA.
AC A6U5E2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, 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}; OrderedLocusNames=Smed_0012;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) 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; CP000738; ABR58872.1; -; Genomic_DNA.
DR RefSeq; WP_011974227.1; NC_009636.1.
DR RefSeq; YP_001325707.1; NC_009636.1.
DR AlphaFoldDB; A6U5E2; -.
DR SMR; A6U5E2; -.
DR STRING; 366394.Smed_0012; -.
DR EnsemblBacteria; ABR58872; ABR58872; Smed_0012.
DR GeneID; 61611140; -.
DR KEGG; smd:Smed_0012; -.
DR PATRIC; fig|366394.8.peg.3067; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_0_2_5; -.
DR OMA; YAYEKIA; -.
DR OrthoDB; 1906715at2; -.
DR Proteomes; UP000001108; 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; Stress response.
FT CHAIN 1..208
FT /note="Protein GrpE"
FT /id="PRO_1000053643"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 208 AA; 22294 MW; 449B287A7B5B7B8E CRC64;
MTDETNKNGP EAAAPEEFDA AAQPETAEEP EADVSAAAPD PLELAKAENA ELRDKYLRLA
AEMDNLRRRT ERDVKDAKSY SVAGFARDML AVSDNLRRAL DAIPADAREA GDAGLKALIE
GVEMTERSML AALERHGVKQ LDPTGQKFDP NFHQAMFEVP NPEVPNNTVV QVVQAGYTIG
ERVLRPAMVG VAKGGPKAAS SEGETPPA
