ID   GRPE_BRADU              Reviewed;         201 AA.
AC   Q79V15; Q9REF1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=blr0676;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110spc4;
RX   PubMed=9108282; DOI=10.1007/s004380050408;
RA   Minder A.C., Narberhaus F., Babst M., Hennecke H., Fischer H.-M.;
RT   "The dnaKJ operon belongs to the sigma32-dependent class of heat shock
RT   genes in Bradyrhizobium japonicum.";
RL   Mol. Gen. Genet. 254:195-206(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(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}.
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DR   EMBL; BA000040; BAC45941.1; -; Genomic_DNA.
DR   EMBL; Y09633; CAB60665.1; -; Genomic_DNA.
DR   RefSeq; NP_767316.1; NC_004463.1.
DR   RefSeq; WP_011083503.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q79V15; -.
DR   SMR; Q79V15; -.
DR   STRING; 224911.27348925; -.
DR   EnsemblBacteria; BAC45941; BAC45941; BAC45941.
DR   GeneID; 64020538; -.
DR   KEGG; bja:blr0676; -.
DR   PATRIC; fig|224911.44.peg.45; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_057217_6_2_5; -.
DR   InParanoid; Q79V15; -.
DR   OMA; YAYEKIA; -.
DR   PhylomeDB; Q79V15; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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..201
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113753"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  21655 MW;  74276120FF14B01D CRC64;
     MTDRDRQPED TTAPTGEPVV SKPYIMPDDP EPGSVELLQK EAAEARDRML RTLAEMENLR
     KRTTKEVADA RLYGITGFAR DVLDIADNLQ RALDAVPAEA RAAADPGLTS LIEGVELTER
     SLLNALEKHG VKKFDPQGQK FDPNFQQAMF EVPDASVPAG TVVQVMQAGY TIGERVLRPA
     LVGVAKGGAK AASAANSNEV N