ID G0LLF7_HALWC Unreviewed; 267 AA.
AC G0LLF7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 ECO:0000313|EMBL:CCC40763.1};
GN OrderedLocusNames=Hqrw_2965 {ECO:0000313|EMBL:CCC40763.1};
OS Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC40763.1, ECO:0000313|Proteomes:UP000007954};
RN [1] {ECO:0000313|EMBL:CCC40763.1, ECO:0000313|Proteomes:UP000007954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16854 / JCM 12705 / C23
RC {ECO:0000313|Proteomes:UP000007954};
RX PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA Rampp M., Oesterhelt D.;
RT "Haloquadratum walsbyi: limited diversity in a global pond.";
RL PLoS ONE 6:E20968-E20968(2011).
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}.
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DR EMBL; FR746099; CCC40763.1; -; Genomic_DNA.
DR RefSeq; WP_014556302.1; NC_017459.1.
DR AlphaFoldDB; G0LLF7; -.
DR GeneID; 12447738; -.
DR KEGG; hwc:Hqrw_2965; -.
DR HOGENOM; CLU_057217_3_0_2; -.
DR OrthoDB; 372230at2157; -.
DR Proteomes; UP000007954; Chromosome.
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 Stress response {ECO:0000256|HAMAP-Rule:MF_01151}.
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..123
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 18..32
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 30020 MW; 55FA7811807A3E23 CRC64;
MSDESTESHQ TAEPSPDSDI SGDEDEDENE REHNMNEEEK HQTKDTHGSS ENPDENNQDA
TTEASSLADQ VAKYDEALAV EVKSLTNEYD EQRERIDELE AALKRSKADF ENYKKRAKKR
EQQIRERATE DFVGRIVGVR DNLVRALEQD SDADIRPGVE STLDEFDRVL EDENVTLINP
ERGDNVDPAQ HEVLMRVDAD LPEGTVAEVF QQGYQMAGTV IQEAQITVST GADITENKNE
NENPDANANT DTDAMKEETN SLENESE
//
