GRPE_FRATH
ID GRPE_FRATH Reviewed; 195 AA.
AC Q2A329;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151};
DE AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151}; OrderedLocusNames=FTL_1190;
OS Francisella tularensis subsp. holarctica (strain LVS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=376619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVS;
RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA Garcia E.;
RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT Strain).";
RL Submitted (MAR-2006) 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:0000255|HAMAP-
CC Rule:MF_01151}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; AM233362; CAJ79629.1; -; Genomic_DNA.
DR RefSeq; WP_003037086.1; NZ_CP009694.1.
DR AlphaFoldDB; Q2A329; -.
DR SMR; Q2A329; -.
DR KEGG; ftl:FTL_1190; -.
DR OMA; YAYEKIA; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 2.30.22.10; -; 1.
DR Gene3D; 3.90.20.20; -; 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; PTHR21237; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF51064; SSF51064; 1.
DR SUPFAM; SSF58014; SSF58014; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Stress response.
FT CHAIN 1..195
FT /note="Protein GrpE"
FT /id="PRO_1000053581"
SQ SEQUENCE 195 AA; 22036 MW; C0B8CFD56568B7DB CRC64;
MSKQEKSNVE DKSLDIETAA QVETAQESAS GALEELSVEE QLERAKDTIK ELEDSCDQFK
DEALRAKAEM ENIRKRAERD VSNARKFGIE KFAKELLPVI DSIEQALKHE VKLEEAIAMK
EGIELTAKML VDILKKNGVE ELDPKGEKFD PNLHEAMAMI PNPEFEDNTI FDVFQKGYML
NGRIVRAAKV VIVKN