Difference between revisions of "GroEL"

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(Basic information/ Evolution)
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:'''  
+
* '''Catalyzed reaction/ biological activity:''' acts as co-repressor for [[HrcA]]
  
 
* '''Protein family:''' chaperonin (HSP60) family (according to Swiss-Prot)
 
* '''Protein family:''' chaperonin (HSP60) family (according to Swiss-Prot)

Revision as of 07:18, 31 May 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
GroEL context.gif
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]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: acts as co-repressor for HrcA
  • Protein family: chaperonin (HSP60) family (according to Swiss-Prot)
  • 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:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:
  • 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

  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