GRPE_PARMW
ID GRPE_PARMW Reviewed; 218 AA.
AC Q7UA77;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SYNW0023;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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; BX569689; CAE06538.1; -; Genomic_DNA.
DR RefSeq; WP_011126901.1; NC_005070.1.
DR AlphaFoldDB; Q7UA77; -.
DR SMR; Q7UA77; -.
DR STRING; 84588.SYNW0023; -.
DR EnsemblBacteria; CAE06538; CAE06538; SYNW0023.
DR KEGG; syw:SYNW0023; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_5_1_3; -.
DR OMA; YAYEKIA; -.
DR OrthoDB; 1906715at2; -.
DR Proteomes; UP000001422; Chromosome.
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..218
FT /note="Protein GrpE"
FT /id="PRO_0000113879"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 24227 MW; 59E5AAFE086DAD8F CRC64;
MSGEASTPAQ DPSVEPLDAA PVAAEPEVMS TETPAEGSLT DPAERLQQLE HELQTLKQEH
ETLQSQYMRI AADFDNFRKR QSRDQEDIRQ QLVCSTLSEI LPVVDNFERA RQQLNPESEE
AQALHRSYQG LYKQLVDVLK QQGVARMEVV GQLFDPTLHE AVLREESTEQ PEDVVIEELQ
RGYHLNGKVL RHALVKVSMG PGPSADAEGA ASAEAEDS