(data stored in SCRATCH zone)

SWISSPROT: A8LDT4_FRASN

ID   A8LDT4_FRASN            Unreviewed;       278 AA.
AC   A8LDT4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-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   OrderedLocusNames=Franean1_0232 {ECO:0000313|EMBL:ABW09699.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09699.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000820; ABW09699.1; -; Genomic_DNA.
DR   RefSeq; WP_012157676.1; NC_009921.1.
DR   STRING; 298653.Franean1_0232; -.
DR   EnsemblBacteria; ABW09699; ABW09699; Franean1_0232.
DR   KEGG; fre:Franean1_0232; -.
DR   eggNOG; ENOG4108093; Bacteria.
DR   eggNOG; COG0576; LUCA.
DR   HOGENOM; HOG000252083; -.
DR   KO; K03687; -.
DR   OMA; LEGPFKA; -.
DR   OrthoDB; 1906715at2; -.
DR   BioCyc; FSP298653:G1G9X-224-MONOMER; -.
DR   Proteomes; UP000001313; 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   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; A8LDT4.
DR   SWISS-2DPAGE; A8LDT4.
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:UP000001313};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|SAAS:SAAS00066909};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00132302}.
FT   COILED       76    103       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   278 AA;  28849 MW;  D3096F91F5940118 CRC64;
     MTSAHGEHRL DDSRAGGDGG PEEPIVKDRR RIDPETGQVR GSAAGAATPG AEPMGPAGAG
     PADSDSELVA SLRGQLGERT ADLQRLKAEF DNYRRRAARE RDAAGDQAVS KLLGGLLGVL
     DDIGRARDHG DLEGPFKAIA ESLETALEST GLERFGTPGE VFDPHLHHAL MHSYRSDVSE
     TTCVEIFRAG YRRGNAVLRA AQVAVAEPSE DGGDALYEDG PDAGISDRVT EVGPPGEYDA
     AEGQPAAGAS PGRENAPLPD DTGSVPGPDR GGPTVSAD
//

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