GRPE_MYCPN
ID GRPE_MYCPN Reviewed; 217 AA.
AC P78017;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=MPN_120;
GN ORFNames=MP034;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=11271496;
RX DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA Frank R.;
RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL Electrophoresis 21:3765-3780(2000).
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:0000305}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; U00089; AAB95682.1; -; Genomic_DNA.
DR PIR; S73360; S73360.
DR RefSeq; NP_109808.1; NC_000912.1.
DR RefSeq; WP_010874477.1; NC_000912.1.
DR AlphaFoldDB; P78017; -.
DR SMR; P78017; -.
DR IntAct; P78017; 1.
DR STRING; 272634.MPN_120; -.
DR EnsemblBacteria; AAB95682; AAB95682; MPN_120.
DR KEGG; mpn:MPN_120; -.
DR PATRIC; fig|272634.6.peg.127; -.
DR HOGENOM; CLU_1271142_0_0_14; -.
DR OMA; LVGFRMF; -.
DR BioCyc; MPNE272634:G1GJ3-200-MON; -.
DR Proteomes; UP000000808; 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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..217
FT /note="Protein GrpE"
FT /id="PRO_0000113821"
SQ SEQUENCE 217 AA; 24706 MW; 3C66757AF4BEBEC3 CRC64;
MSENSLTITE ILSSIRTLLV KHNKAKVTQI EKELLQAVAE LEKKFKQQVQ NFNELQQKIP
NLQKVNEEFR LKVEKIQEEA QKKIQEKVAE LTIKSKEELE NAKKYVIEKS IDQPLIIIDQ
FEIALSYAQK DPQVKNYTTG FNMVLDAFSR WLEGFGVTKI AIEPGAQFDE KVMAALEVVP
SDQPANTVVK VSKSGYKLHD KVIRFASVVV SQGNKTE