ID A0A1J4XW82_9BACT Unreviewed; 169 AA.
AC A0A1J4XW82;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 03-MAY-2023, entry version 22.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU000639};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151};
GN ORFNames=AUJ30_00685 {ECO:0000313|EMBL:OIO65619.1};
OS Candidatus Wolfebacteria bacterium CG1_02_39_135.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=1805425 {ECO:0000313|EMBL:OIO65619.1, ECO:0000313|Proteomes:UP000182693};
RN [1] {ECO:0000313|EMBL:OIO65619.1, ECO:0000313|Proteomes:UP000182693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_39_135 {ECO:0000313|EMBL:OIO65619.1};
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. {ECO:0000256|HAMAP-
CC Rule:MF_01151, ECO:0000256|RuleBase:RU000639}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|HAMAP-Rule:MF_01151, 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:OIO65619.1}.
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DR EMBL; MNWX01000013; OIO65619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4XW82; -.
DR STRING; 1805425.AUJ30_00685; -.
DR Proteomes; UP000182693; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01151};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 169 AA; 19530 MW; 0F91026AAE84CD1B CRC64;
MAEEIQKNNE EKLEEKEKPE EIDELSKCQK ERDEYLDGWK RAKADLINYK KDEAKRFEAI
VKFSNESLVR ELINVLDSFD LALVALENEA DLKKERGLYL IRQQLEDILK QNGLERIIIS
VGQPFDPALQ EAVAEVESDK PSSTIIEEVE RGYLLNGKLI RPARVKVSK
//
