ID L9X8F7_9EURY Unreviewed; 383 AA.
AC L9X8F7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151};
GN ORFNames=C493_07564 {ECO:0000313|EMBL:ELY57731.1};
OS Natronolimnohabitans innermongolicus JCM 12255.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronolimnohabitans.
OX NCBI_TaxID=1227499 {ECO:0000313|EMBL:ELY57731.1, ECO:0000313|Proteomes:UP000011602};
RN [1] {ECO:0000313|EMBL:ELY57731.1, ECO:0000313|Proteomes:UP000011602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12255 {ECO:0000313|EMBL:ELY57731.1,
RC ECO:0000313|Proteomes:UP000011602};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(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. {ECO:0000256|HAMAP-
CC Rule:MF_01151}.
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:ELY57731.1}.
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DR EMBL; AOHZ01000040; ELY57731.1; -; Genomic_DNA.
DR RefSeq; WP_007258814.1; NZ_AOHZ01000040.1.
DR AlphaFoldDB; L9X8F7; -.
DR STRING; 1227499.C493_07564; -.
DR PATRIC; fig|1227499.3.peg.1522; -.
DR eggNOG; arCOG04772; Archaea.
DR OrthoDB; 372230at2157; -.
DR Proteomes; UP000011602; 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.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01151};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Reference proteome {ECO:0000313|Proteomes:UP000011602};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151}.
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..183
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 245..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 40962 MW; 74CBAE137B48D8C6 CRC64;
MSEDEGTNAD AQGVPSEDHS DGGDPADVEA ATGADESDGA SASDTDAATE STTDDSNESE
AAVDDATTAS GDGAAPETSE DIQDLLDQIT EYDDDLAHQV NAVVEEARDL NGTVADQRAE
LEDLSERVEE QAETIDKLQS ELEAREAEVD EYEAEVEDLT SRLKRKQADF QNYKKRAKKR
QDQIKDRATE DLVERLLGVR DNLKRALEEE HGDVESLREG VEMTMKEFDR ILEDENVSEI
DPEPGTETDP QRHEVMMRVD SAQPEGTVAD VYTPGYEMGD KVIQNAQVTV SNGELEGEDE
DADSDADGAG GTGDENADST APESDESDSA ADDDSAGGAD SEDGTGDDDE ASEDDDAIEL
GGEVAGDDDL EETDASTDGD ESN
//
