ID   GRPE_MYCPU              Reviewed;         194 AA.
AC   Q98R67;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein GrpE;
DE   AltName: Full=HSP-70 cofactor;
GN   Name=grpE; OrderedLocusNames=MYPU_1430;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC13316.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL445563; CAC13316.1; ALT_INIT; Genomic_DNA.
DR   PIR; G90529; G90529.
DR   AlphaFoldDB; Q98R67; -.
DR   SMR; Q98R67; -.
DR   STRING; 272635.MYPU_1430; -.
DR   EnsemblBacteria; CAC13316; CAC13316; CAC13316.
DR   KEGG; mpu:MYPU_1430; -.
DR   eggNOG; COG0576; Bacteria.
DR   HOGENOM; CLU_070790_0_0_14; -.
DR   Proteomes; UP000000528; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR013805; GrpE_coiled_coil.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   SUPFAM; SSF58014; SSF58014; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..194
FT                   /note="Protein GrpE"
FT                   /id="PRO_0000113822"
SQ   SEQUENCE   194 AA;  22621 MW;  5109E4F8536E156D CRC64;
     MKNKILVKNN ELTVDISAFD DKDEVLSLQR KNFNLILGKD SFLRGFDANL IGQKSLPLYE
     FSMVIPSDFK DEKLRGKTLD FKVHNKAKIK VNSETNLDKE KIKSLEKELA NQKEKNALLL
     LDNVKLKSEK EKIIKDFKDE IKTFENRARE KIAEKLNLEK QLLENKFEDF KKYGSQKIFE
     SIMPIIQNLL VAIE