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Database: UniProt
Entry: GRPE_METST
LinkDB: GRPE_METST
Original site: GRPE_METST 
ID   GRPE_METST              Reviewed;         173 AA.
AC   Q2NE66;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=Msp_1518;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57887.1; -; Genomic_DNA.
DR   RefSeq; WP_011407086.1; NC_007681.1.
DR   AlphaFoldDB; Q2NE66; -.
DR   SMR; Q2NE66; -.
DR   STRING; 339860.Msp_1518; -.
DR   GeneID; 41326094; -.
DR   KEGG; mst:Msp_1518; -.
DR   eggNOG; arCOG04772; Archaea.
DR   HOGENOM; CLU_057217_5_2_2; -.
DR   OrthoDB; 372230at2157; -.
DR   Proteomes; UP000001931; 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:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00446; GrpE; 1.
DR   Gene3D; 3.90.20.20; -; 1.
DR   Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 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; GRPE PROTEIN; 1.
DR   PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01025; GrpE; 1.
DR   PRINTS; PR00773; GRPEPROTEIN.
DR   SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR   SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR   PROSITE; PS01071; GRPE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..173
FT                   /note="Protein GrpE"
FT                   /id="PRO_1000053606"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   173 AA;  20724 MW;  5F0D28A299189401 CRC64;
     MTEEEKTKSE AEEIEQNNKE EEQEKSVEEL LEEKEQEIQQ YKDKLQRIHA DFENFKKRSI
     KEKQEFVKFA NEGLILKVLE AYEDLERALE VKEDKNLREG VELIYKKLTK ILEDEGVEPI
     ETKNQKFDPY KHEALMTEDN DDYENNEIIQ DLQKGYTLNS KVIRYSKVKV CKK
//
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