Difference between revisions of "GroEL"
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[groES]]'', ''[[ydiM]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[groES]]'', ''[[ydiM]]'' | ||
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− | |style="background:#FAF8CC;" align="center"|'''[http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB12422]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
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|colspan="2" | '''Genetic context''' <br/> [[Image:groEL_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:groEL_context.gif]] |
Revision as of 04:25, 17 April 2009
- Description: chaperonin
Gene name | groEL |
Synonyms | |
Essential | yes PubMed |
Product | chaperonin |
Function | protein folding and re-folding |
MW, pI | 57 kDa, 4.531 |
Gene length, protein length | 1632 bp, 544 aa |
Immediate neighbours | groES, ydiM |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Wolfgang Schumann, Bayreuth University, Germany Homepage
Your additional remarks
References
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Lévine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6: 2157-2173 PubMed
- Mogk, A., Homuth, G., Scholz, C., Kim, L., Schmid, F. X., and Schumann, W. (1997) The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J 16, 4579-4590. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed