CcpA
- Description: carbon catabolite control protein A, involved in glucose regulation of many genes; mediates carbon catabolite repression (CCR)of catabolic genes and the positive regulation of genes involved in excretion of excess carbon
Gene name | ccpA |
Synonyms | graR, alsA, amyR |
Essential | no |
Product | transcriptional regulator |
Function | mediates carbon catabolite repression (CCR) |
MW, pI | 36,8 kDa, 5.06 |
Gene length, protein length | 1002 bp, 334 amino acids |
Immediate neighbours | aroA, motP |
Gene sequence (+200bp) | Protein sequence |
Genetic context File:GenE context.gif |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: transcriptional regulator
- Protein family: LacI family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- HTH lacI-type Domain (1 – 58)
- DNA binding Domain (6 – 25)
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number:
Additional information
Expression and regulation
- Operon: ccpA motPS PubMed
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
Labs working on this gene/protein
Your additional remarks
References
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
- Terahara et al. (2006) An intergenic stem-loop mutation in the Bacillus subtilis ccpA-motPS operon increases motPS transcription and the MotPS contribution to motility J Bacteriol. 188(7): 2701-5. PubMed
- Mahr K, Esteban CD & Hillen W (2002) Cross communication between components of carbon catabolite repression of Lactobacillus casei and Bacillus megaterium J Mol Microbiol Biotechnol. 4(5): 489-94. PubMed
- Juy M, Penin F, Favier A (2003)Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr. J Mol Biol. 332(4):767-76. PubMed