GRPE_PARTM
ID GRPE_PARTM Reviewed; 224 AA.
AC Q9KWS8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 84.
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};
OS Parageobacillus thermoglucosidasius (Geobacillus thermoglucosidasius).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=1426;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15188890; DOI=10.1023/a:1002483620374;
RA Watanabe K., Iwashiro T., Suzuki Y.;
RT "Features of dnaK operon genes of the obligate thermophile Bacillus
RT thermoglucosidasius KP1006.";
RL Antonie Van Leeuwenhoek 77:241-250(2000).
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; AB017035; BAB03214.1; -; Genomic_DNA.
DR RefSeq; WP_042383496.1; NZ_LAKX01000006.1.
DR AlphaFoldDB; Q9KWS8; -.
DR SMR; Q9KWS8; -.
DR STRING; 1426.AOT13_16995; -.
DR GeneID; 56927135; -.
DR PATRIC; fig|1426.34.peg.3919; -.
DR eggNOG; COG0576; Bacteria.
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..224
FT /note="Protein GrpE"
FT /id="PRO_0000113744"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 224 AA; 26077 MW; B6275279B33A7462 CRC64;
MEKERDVAQE QATYEQESPN AERQEELKEN EHQEKNAPEE QEKVREENGR QDAQKDEIGD
PEKAKEEQNE ELAAANAKIA ELEAKIKEME NRYLRLYADF ENFRRRTRRE MEAAEKYRAQ
SLVSDLLPVL DNFERALKIK AEDEQAKSIL QGMEMVYRSV LDALKKEGVE AIEAVGKPFD
PHLHQAVMQV EDSNYEPNTV VEELQKGYKL KDRVIRPAMV KVSQ
