CggR

• Description: repressor of the glycolytic gapA operon
  
  

Gene name	cggR
Synonyms	yvbQ
Essential	no
Product	write here
Function	write here
MW, pI	xx,x kDa, y.yy
Gene length, protein length	aaa bp, bbb amino acids
Immediate neighbours	genA, genB
Gene sequence (+200bp)	Protein sequence
Genetic context File:GenE context.gif

The gene

Basic information

• Coordinates:

Database entries

• DBTBS entry: [1]

• SubtiList entry:

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry:

• KEGG entry:

• E.C. number:

Expression and regulation

• Operon:
  • cggR-gapA-pgk-tpiA-pgm-eno
  • cggR-gapA

The primary mRNAs of the operon are highly unstable. The primary mRNA is subject to processing at the very end of the cggR open reading frame. This results in stable mature gapA and gapA-pgk-tpiA-pgm-eno mRNAs. The processing event requires the Rny protein.

• Sigma factor: SigA

• Regulation: CggR represses the operon in the absence of glycolytic sugars

• Regulatory mechanism: repression

• Database entries: DBTBS

• Additional information:

References

1. Doan, T., and S. Aymerich. 2003. Regulation of the central glycolytic pathways in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate. Mol. Microbiol. 47: 1709-1721. PubMed
2. Fillinger, S., Boschi-Muller, S., Azza, S., Dervyn, E., Branlant, G., and Aymerich, S. (2000) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275, 14031-14037. PubMed
3. Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol Microbiol 41, 409-422.PubMed
4. Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002). Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol Microbiol 45, 543-553.PubMed
5. Meinken, C., Blencke, H. M., Ludwig, H., and Stülke, J. (2003) Expression of the glycolytic gapA operon in Bacillus subtilis: differential synthesis of proteins encoded by the operon. Microbiology 149, 751-761. PubMed