ID E4Q8Y6_CALH1 Unreviewed; 225 AA.
AC E4Q8Y6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 ECO:0000313|EMBL:ADQ06905.1};
GN OrderedLocusNames=Calhy_1185 {ECO:0000313|EMBL:ADQ06905.1};
OS Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 / 108).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632292 {ECO:0000313|EMBL:ADQ06905.1, ECO:0000313|Proteomes:UP000006890};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=108;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor hydrothermalis 108.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ06905.1, ECO:0000313|Proteomes:UP000006890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18901 / VKM B-2411 / 108
RC {ECO:0000313|Proteomes:UP000006890};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(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, 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}.
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DR EMBL; CP002219; ADQ06905.1; -; Genomic_DNA.
DR RefSeq; WP_013403085.1; NC_014652.1.
DR AlphaFoldDB; E4Q8Y6; -.
DR STRING; 632292.Calhy_1185; -.
DR KEGG; chd:Calhy_1185; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_5_1_9; -.
DR OrthoDB; 9812586at2; -.
DR Proteomes; UP000006890; 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.
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..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 225 AA; 26080 MW; F1616A218880865F CRC64;
MLDMENKDLK SEEVNSSEAQ TLEETNSEGK NENMQHSQEP QEDAAKTQEN DGSNESSEDI
EVEPHQEDTV ETLKKQLEEK EREVEEYKSL CQRIAADFDN YKKRIAKDKE NMYYEVVADV
VGKLLPIVDN FERAIDSAKN SRDKNDELLK GLEMIKKQID DIFSKLGVEP IEALNKEFDP
YLHNAIMHVE DERYGKNVVI EEFQKGYKIK DRVIRYSLVK VANAN
//
