ID A0A060HU74_9ARCH Unreviewed; 191 AA.
AC A0A060HU74;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Protein GrpE {ECO:0000256|RuleBase:RU000639};
GN Name=grpE {ECO:0000313|EMBL:AIC16662.1};
GN ORFNames=NVIE_2456 {ECO:0000313|EMBL:AIC16662.1};
OS Nitrososphaera viennensis EN76.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=926571 {ECO:0000313|EMBL:AIC16662.1, ECO:0000313|Proteomes:UP000027093};
RN [1] {ECO:0000313|EMBL:AIC16662.1, ECO:0000313|Proteomes:UP000027093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EN76 {ECO:0000313|EMBL:AIC16662.1};
RX PubMed=24907263; DOI=10.1099/ijs.0.063172-0;
RA Stieglmeier M., Klingl A., Alves R.J., Rittmann S.K., Melcher M.,
RA Leisch N., Schleper C.;
RT "Nitrososphaera viennensis gen. nov., sp. nov., an aerobic and mesophilic,
RT ammonia-oxidizing archaeon from soil and a member of the archaeal phylum
RT Thaumarchaeota.";
RL Int. J. Syst. Evol. Microbiol. 64:2738-2752(2014).
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; CP007536; AIC16662.1; -; Genomic_DNA.
DR RefSeq; WP_075055380.1; NZ_CP007536.1.
DR AlphaFoldDB; A0A060HU74; -.
DR STRING; 926571.NVIE_2456; -.
DR GeneID; 74947639; -.
DR KEGG; nvn:NVIE_2456; -.
DR HOGENOM; CLU_057217_4_2_2; -.
DR OrthoDB; 372230at2157; -.
DR Proteomes; UP000027093; Chromosome.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000027093};
KW Stress response {ECO:0000256|RuleBase:RU000639}.
FT COILED 11..41
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 191 AA; 21090 MW; D99F49FBA9F1D4A7 CRC64;
MVATAATDDD TEEAQQQIDE TEELRKELAA AKEAAEGNLN KLKYLMADFD NYRKQMEKHA
ASRVETIKAE LLLKFLNIRD DYQRAIEGAR QKKSEPAVIE GLEGILKNID SLLSSEGVRP
IEAVGTPFDP NVHDAIAFSP REDAEENTVT AEIRRGYMLN GKVLRPSMVE IARKIVKNSD
SANNGGAGGE E
//