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GRPE_MESFL
ID   GRPE_MESFL              Reviewed;         187 AA.
AC   Q6F148;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Mfl416;
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC   Mesoplasma.
OX   NCBI_TaxID=265311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL   Submitted (JUN-2004) 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; AE017263; AAT75775.1; -; Genomic_DNA.
DR   RefSeq; WP_011183315.1; NC_006055.1.
DR   RefSeq; YP_053659.1; NC_006055.1.
DR   AlphaFoldDB; Q6F148; -.
DR   SMR; Q6F148; -.
DR   STRING; 265311.Mfl416; -.
DR   EnsemblBacteria; AAT75775; AAT75775; Mfl416.
DR   GeneID; 2897591; -.
DR   KEGG; mfl:Mfl416; -.
DR   PATRIC; fig|265311.5.peg.417; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_057217_4_2_14; -.
DR   OMA; YAYEKIA; -.
DR   Proteomes; UP000006647; 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; Reference proteome; Stress response.
FT   CHAIN           1..187
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113811"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   187 AA;  21362 MW;  C71544F5390F38DA CRC64;
     MNNEKELKKE ETSVENKEKK VATEEIKKEK KDYKKIIQDL EKQIESCQKE IEFQKSLRNA
     DIANLTKKRN EQEALVRKYG SSNLAEDLIK PIDLLKKVVE TPTDIPELQN YLMGFKMIIS
     QIENAFETNG IKAMGVKAGD EFDSSFHEAN ESLENSGMES NKIVSVISDG YMIHDRVLIH
     AIVKVAK
 
 
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