(data stored in SCRATCH zone)

SWISSPROT: C3MEJ3_SINFN

ID   C3MEJ3_SINFN            Unreviewed;       222 AA.
AC   C3MEJ3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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:ACP23816.1};
GN   OrderedLocusNames=NGR_c00120 {ECO:0000313|EMBL:ACP23816.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23816.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23816.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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:SAAS00646558}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|SAAS:SAAS00646548}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
CC       ECO:0000256|SAAS:SAAS00646554}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|HAMAP-
CC       Rule:MF_01151, ECO:0000256|RuleBase:RU004478,
CC       ECO:0000256|SAAS:SAAS00646546}.
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DR   EMBL; CP001389; ACP23816.1; -; Genomic_DNA.
DR   RefSeq; WP_012706601.1; NC_012587.1.
DR   RefSeq; YP_002824569.1; NC_012587.1.
DR   SMR; C3MEJ3; -.
DR   STRING; 394.NGR_c00120; -.
DR   EnsemblBacteria; ACP23816; ACP23816; NGR_c00120.
DR   GeneID; 7790591; -.
DR   KEGG; rhi:NGR_c00120; -.
DR   PATRIC; fig|394.7.peg.2802; -.
DR   eggNOG; ENOG4105K90; Bacteria.
DR   eggNOG; COG0576; LUCA.
DR   HOGENOM; HOG000252083; -.
DR   KO; K03687; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; POG091H00J8; -.
DR   Proteomes; UP000001054; 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   PROSITE; PS01071; GRPE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MEJ3.
DR   SWISS-2DPAGE; C3MEJ3.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00646544};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|SAAS:SAAS00646553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW   ECO:0000256|RuleBase:RU000639, ECO:0000256|SAAS:SAAS00646545}.
FT   COILED       56     83       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   222 AA;  23803 MW;  9F86F350B7190337 CRC64;
     MMPNTPKTRH SENVMTDETN KNGTEAAAPE EIVKATGPEA AEKPEAGASA AGPDPLELAK
     AESADLRDKY LRLAAEMDNL RRRTERDVKD AKSYSVAGFA RDMLAVSDNL RRALEAIPAE
     ARESGDAGLT ALIEGVEMTE RSMLAALERH GVKQLDPTGQ RFDPNFHQAM FEVPNPEVPN
     NTVVQVVQAG YTIGERVLRP AMVGVAKGGP KIVAAESETP AA
//

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