GroEL

• 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
Gene sequence (+200bp)	Protein sequence
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates:

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed, PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry:

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• 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

References

1. Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
2. 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
3. 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
4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed