ID   GRPE_BLOPB              Reviewed;         195 AA.
AC   Q492C7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=BPEN_564;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41174.1; -; Genomic_DNA.
DR   RefSeq; WP_011283085.1; NC_007292.1.
DR   AlphaFoldDB; Q492C7; -.
DR   SMR; Q492C7; -.
DR   STRING; 291272.BPEN_564; -.
DR   EnsemblBacteria; AAZ41174; AAZ41174; BPEN_564.
DR   KEGG; bpn:BPEN_564; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_057217_6_0_6; -.
DR   OMA; YAYEKIA; -.
DR   BioCyc; CBLO291272:BPEN_RS02785-MON; -.
DR   Proteomes; UP000007794; 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..195
FT                   /note="Protein GrpE"
FT                   /id="PRO_1000137542"
SQ   SEQUENCE   195 AA;  22483 MW;  B947D8A890157FC8 CRC64;
     MIDNNVKNNI DESTLQNEKI EKEELLESVS TVDNVIDPKN DQIIKLKIQL AQLQEHERNT
     VLRLTAEIEN IRRRNTQEIE KIHKFGLERF IFELLPVIDN LERTMSISDN SNTLLSAIIE
     GIELTLKSFL DTVHKFGLKS IYEINVPFNP EIHQAISIIE SEDHKPNQVL TMIQKGYILN
     GRLIRPAMVT VSQSK