ID A0A2K5ANN1_9ARCH Unreviewed; 188 AA.
AC A0A2K5ANN1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Protein GrpE {ECO:0000256|RuleBase:RU000639};
GN ORFNames=NCAV_0044 {ECO:0000313|EMBL:SPC33244.1};
OS Candidatus Nitrosocaldus cavascurensis.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Candidatus Nitrosocaldales;
OC Candidatus Nitrosocaldaceae; Candidatus Nitrosocaldus.
OX NCBI_TaxID=2058097 {ECO:0000313|EMBL:SPC33244.1, ECO:0000313|Proteomes:UP000236248};
RN [1] {ECO:0000313|Proteomes:UP000236248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCU2 {ECO:0000313|Proteomes:UP000236248};
RA Kerou L M.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT981265; SPC33244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K5ANN1; -.
DR KEGG; ncv:NCAV_0044; -.
DR Proteomes; UP000236248; Chromosome ncav.
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}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 21094 MW; F15AFBB924354529 CRC64;
MSIGDKNNGD TVNSDASKIN SEEAMVGGSS KEEVEMLKSA LKEYESRYKY LLADYDNYRK
RVEREAEYRV RQSIESFVLK LLSLRDDFMR AVDAARKSAD KHVVEGLEGV LKNLDGILRD
AGVVEIPAVG KTFNPNMHEA VSFIYNAELP DLTVTSEIRK GYMMNDKVIR PSLVEVSRRP
VQEGGGEP
//