ID   GRPE_MYCCT              Reviewed;         200 AA.
AC   P71499; Q2SSB1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 110.
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=MCAP_0368;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8995799; DOI=10.1099/00207713-47-1-38;
RA   Falah M., Gupta R.S.;
RT   "Phylogenetic analysis of mycoplasmas based on Hsp70 sequences: cloning of
RT   the dnaK (hsp70) gene region of Mycoplasma capricolum.";
RL   Int. J. Syst. Bacteriol. 47:38-45(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC01487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; U51235; AAB09429.1; -; Genomic_DNA.
DR   EMBL; CP000123; ABC01487.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041159928.1; NC_007633.1.
DR   AlphaFoldDB; P71499; -.
DR   SMR; P71499; -.
DR   EnsemblBacteria; ABC01487; ABC01487; MCAP_0368.
DR   GeneID; 23778676; -.
DR   KEGG; mcp:MCAP_0368; -.
DR   HOGENOM; CLU_057217_4_2_14; -.
DR   OrthoDB; 1556796at2; -.
DR   PhylomeDB; P71499; -.
DR   Proteomes; UP000001928; 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..200
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113814"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        122..124
FT                   /note="QAY -> LRN (in Ref. 1; AAB09429)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="K -> KINKNNN (in Ref. 1; AAB09429)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   200 AA;  23066 MW;  3E231C444CC26E4F CRC64;
     MTEELKNKKN NKNYYSQNKN KTKAEFQKPH VKKNQYLKLK TKLDTALLEV QNLKDLNETL
     KKDIESERQL NLAEISNLTK KYNQKEIEIQ KYGASKLARD LIQPLEILKK VVNAPNNNEV
     VQAYVKGFEM IVSQINNVLE SHHIKAMNVK VGDMFNPHLH DANEAVESDE YKTNQIVGVL
     SDGYMIHDKV LIYAIVKVAK