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Database: UniProt
Entry: R6KPL2_9CLOT
LinkDB: R6KPL2_9CLOT
Original site: R6KPL2_9CLOT 
ID   R6KPL2_9CLOT            Unreviewed;       187 AA.
AC   R6KPL2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ORFNames=BN573_01618 {ECO:0000313|EMBL:CDB75455.1};
OS   Clostridium sp. CAG:265.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262787 {ECO:0000313|EMBL:CDB75455.1, ECO:0000313|Proteomes:UP000018277};
RN   [1] {ECO:0000313|EMBL:CDB75455.1, ECO:0000313|Proteomes:UP000018277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:265 {ECO:0000313|Proteomes:UP000018277};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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, 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}.
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:CDB75455.1}.
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DR   EMBL; CBEC010000069; CDB75455.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6KPL2; -.
DR   Proteomes; UP000018277; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000018277};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639}.
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   187 AA;  21229 MW;  9D9A1CBFB4E944F6 CRC64;
     MEENKDLNEE IIDEAEATTE STEEVNEAEN NEETDLALVK KLKEENDKLS KEVEAFKDRL
     LRVTAEYENF RKRTAKEKEG IYADACADVL KEVIPTIDNL ERALAVDGSV EDLKKGIEMT
     IKGFQTSLEK LGVEEISVEE GFDPNMHQAV MHIQDENLDK NVVAEVFLKG YKKGDKVIRY
     SMVKVAN
//
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