ID A0A2L2XD04_9FIRM Unreviewed; 155 AA.
AC A0A2L2XD04;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=DCCM_2709 {ECO:0000313|EMBL:GBF33603.1};
OS Desulfocucumis palustris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfocucumaceae;
OC Desulfocucumis.
OX NCBI_TaxID=1898651 {ECO:0000313|EMBL:GBF33603.1, ECO:0000313|Proteomes:UP000239549};
RN [1] {ECO:0000313|Proteomes:UP000239549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAW-5 {ECO:0000313|Proteomes:UP000239549};
RA Watanabe M., Kojima H., Fukui M.;
RT "Genome sequence of Desulfocucumis palustris strain NAW-5.";
RL Submitted (FEB-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. {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:GBF33603.1}.
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; BFAV01000104; GBF33603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2XD04; -.
DR OrthoDB; 9812586at2; -.
DR Proteomes; UP000239549; 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:SF40; CELL CYCLE AND APOPTOSIS REGULATOR PROTEIN 2; 1.
DR PANTHER; PTHR21237; GRPE PROTEIN; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Reference proteome {ECO:0000313|Proteomes:UP000239549};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000313|EMBL:GBF33603.1}.
SQ SEQUENCE 155 AA; 17859 MW; CF3D2CB33763ED0D CRC64;
MNEQPQRAKD LEEANTLRRE LAEEKNRHLR TLADFDNYRK RVEREAEAGS LRGKKELVRD
LLSVLDIFER VPAQIQDEEI RRGLLLVQRQ LRDTLDRHGL ERVESLGRPF DPAGHEGVGY
VQSNTCPPGH VAEELSPGYR FGNELLRPAR VLVVK
//
