(data stored in SCRATCH zone)

SWISSPROT: A5GPW5_SYNR3

ID   A5GPW5_SYNR3            Unreviewed;       246 AA.
AC   A5GPW5;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 68.
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   ECO:0000313|EMBL:CAK26924.1};
GN   OrderedLocusNames=SynRCC307_0021 {ECO:0000313|EMBL:CAK26924.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK26924.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic
CC       and heat shock by preventing the aggregation of stress-denatured
CC       proteins, in association with DnaK and GrpE. It is the nucleotide
CC       exchange factor for DnaK and may function as a thermosensor.
CC       Unfolded proteins bind initially to DnaJ; upon interaction with
CC       the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC       in the formation of a stable complex. GrpE releases ADP from DnaK;
CC       ATP binding to DnaK triggers the release of the substrate protein,
CC       thus completing the reaction cycle. Several rounds of ATP-
CC       dependent interactions between DnaJ, DnaK and GrpE are required
CC       for fully efficient folding. {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00067045}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|SAAS:SAAS00066998}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|SAAS:SAAS00067044}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|HAMAP-
CC       Rule:MF_01151, ECO:0000256|RuleBase:RU004478,
CC       ECO:0000256|SAAS:SAAS00562011}.
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DR   EMBL; CT978603; CAK26924.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0021; -.
DR   EnsemblBacteria; CAK26924; CAK26924; SynRCC307_0021.
DR   KEGG; syr:SynRCC307_0021; -.
DR   eggNOG; ENOG4107Z9D; Bacteria.
DR   eggNOG; COG0576; LUCA.
DR   KO; K03687; -.
DR   OMA; YAYEKIA; -.
DR   Proteomes; UP000001115; 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;
DR   PRODOM; A5GPW5.
DR   SWISS-2DPAGE; A5GPW5.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00132311};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|SAAS:SAAS00066909};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00132302,
KW   ECO:0000313|EMBL:CAK26924.1}.
FT   COILED       77     97       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   246 AA;  26696 MW;  8BA154E4197571D3 CRC64;
     MIQGSASQQH GRTARVAPMT AEPPTSPSPS EAEVSVEDQQ QPMAEAQVEQ PAADAAAAEP
     ETTAEAPEAT AESGDGAAAL EAELTALRQE HETVRSQYMR IAADFDNFRK RQQRDAEDLK
     LQLTCSTLGE ILPVVDNFER ARQQLNPEGE EAQALHRSYQ GLYKQLVDVL KQLGVSPMRV
     EGEPFDPTLH EAVLREPSDA HSEDVVMEEL QRGYHLDGRV LRHAMVKVSM GPGPAAAPES
     APAEGN
//

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