GRPE_METMZ
ID GRPE_METMZ Reviewed; 209 AA.
AC P0CW10; P42367;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
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 Methanosarcina mazei (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2209;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=S-6;
RX PubMed=7517454; DOI=10.1006/jmbi.1994.1422;
RA Conway de Macario E., Dugan C.B., Macario A.J.L.;
RT "Identification of a grpE heat-shock gene homolog in the archaeon
RT Methanosarcina mazei.";
RL J. Mol. Biol. 240:95-101(1994).
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 -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:7517454}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; X74353; CAA52395.1; -; Genomic_DNA.
DR PIR; S46379; S46379.
DR RefSeq; WP_048038245.1; NZ_JJRB01000013.1.
DR AlphaFoldDB; P0CW10; -.
DR SMR; P0CW10; -.
DR GeneID; 44088193; -.
DR GeneID; 66135468; -.
DR OMA; LEGPFKA; -.
DR OrthoDB; 114121at2157; -.
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 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; Stress response.
FT CHAIN 1..209
FT /note="Protein GrpE"
FT /id="PRO_0000113910"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 23995 MW; DE3A2FBBC1C9D381 CRC64;
MKKSRKKENM DSKERNQKEA ERSEARNSES PAEKAGETKV SPENEPSSPE AEKNPEEACR
EENEILKDQL FRLAADFDNF RKRTARQMEE NRKSVLEQVL LDFVEVTDNF DRAIKSARTA
EDMGPIVSGI EQLSKQFFSI LEKYGLERVK CEKAGEFDPH RHEAIHHIET SEVPDNTIVE
IYKEGYALNE KVVRPALVSV ARSPEEAEK
