ID A0A1J4UMB7_9ARCH Unreviewed; 187 AA.
AC A0A1J4UMB7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Protein GrpE {ECO:0000256|RuleBase:RU000639};
GN ORFNames=AUJ13_00675 {ECO:0000313|EMBL:OIO25898.1};
OS Candidatus Micrarchaeota archaeon CG1_02_49_24.
OC Archaea; Candidatus Micrarchaeota.
OX NCBI_TaxID=1805248 {ECO:0000313|EMBL:OIO25898.1, ECO:0000313|Proteomes:UP000181889};
RN [1] {ECO:0000313|EMBL:OIO25898.1, ECO:0000313|Proteomes:UP000181889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_49_24 {ECO:0000313|EMBL:OIO25898.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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.
CC {ECO:0000256|RuleBase:RU000639}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|RuleBase:RU004478}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIO25898.1}.
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DR EMBL; MNVF01000016; OIO25898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4UMB7; -.
DR Proteomes; UP000181889; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000639};
KW Stress response {ECO:0000256|RuleBase:RU000639}.
SQ SEQUENCE 187 AA; 20624 MW; 0ED255EF160B3FF0 CRC64;
MVSDKKNTPT KDTMDGEPCE GCECDGSCEK KEAPAVDDKI DYVDLYARKA AELENYKKLA
GKQLDAQKFR AKEVLVRKFL PVMDDLEAGL AADGEHKGLH ALQDKLKAIL ASEGLNEIEI
PAGGKFDPYI HEVVQEMESE KENGTILQVI RKGYSFDGNV IRAAMVIVAK KSMDIDSTNN
STNKTEI
//
