AhrC

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  • Description: AhrC represses the genes for arginine biosynthesis and activates the genes for arginine catabolism.

Gene name ahrC
Synonyms argR
Essential no
Product transcriptional regulator
Function transcriptional regulator of arginine metabolic genes
MW, pI 16,7 kDa, 5.52
Gene length, protein length 447 bp, 149 amino acids
Immediate neighbours yqxC, recN
Gene sequence (+200bp) Protein sequence
Genetic context
File:GenE context.gif












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 activator/ repressor of genes involved in arginine metabolism
  • Protein family: ArgR family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): L-arginine is the co-factor required for transcription repression/ activation
  • Effectors of protein activity:
  • Interactions:
  • Localization: Cytoplasm

Database entries

  • Swiss prot entry: [3]
  • KEGG entry: [4]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

Labs working on this gene/protein

Simon Phillips, Leeds University, UK Homepage

Michel Debarbouille, Pasteur Institute, Paris, France Homepage

Your additional remarks

References

  1. Van Hoy BE et al. (1990) Characterization of the spoIVB and recN loci of Bacillus subtilis J Bacteriol. 172: 1306-1311. PubMed
  2. Heidrich et al. (2006) The small untranslated RNA SR1 from the Bacillus subtilis genome is involved in the regulation of arginine catabolism. Mol. Microbiol. 62: 520-536. PubMed
  3. Heidrich et al. (2007) In vitro analysis of the interaction between the small RNA SR1 and its primary target ahrC mRNA. Nucl. Acids Res. 35: 4331-4346. PubMed
  4. Garnett et al. (2008) Structure and function of the arginine repressor-operator complex from Bacillus subtilis. J. Mol. Biol. 379: 284-298. PubMed
  5. Garnett et al. (2007) Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine. Acta Cryst. Sect. F. 63: 918-921. PubMed
  6. Garnett et al. (2007) A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis. Acta Cryst. Sect. F. 63: 914-917. PubMed
  7. Dennis et al. (2002) The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis. Acta Cryst. Sect. D. 58:421-430. PubMed
  8. Makarova et al. (2001) Conservation of the binding site for the arginine repressor in all bacterial lineages. Genome Biol. 2: RESEARCH0013. PubMed
  9. Miller et al. (1997) Operator interactions by the Bacillus subtilis arginine repressor/ activator, AhrC: novel positioning and DNA-mediated assembly of a transcriptional activator at catabolic sites. Mol. Microbiol. 26: 37-48. PubMed
  10. Klingel et al. (1995) A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/ activator of arginine metabolism. Mol. Gen. Genet. 248:329-340. PubMed
  11. Czaplewski et al. (1992) Purification and initial characterization of AhrC: the regulator of arginine metabolism genes in Bacillus subtilis. Mol. Microbiol. 6:267-275. PubMed
  12. North et al. (1989) Nucleotide sequence of a Bacillus subtilis arginine regulatory gene and homology of its product to the Escherichia coli arginine repressor. Gene 80:29-38. 2507400 PubMed