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Description: transcriptional regulator of the ArgR family, AhrC represses the genes for arginine biosynthesis and activates the genes for arginine catabolism.

Name: ahrC
Locus: BSU24250BsubCyc
pI: 5.0
MW: 16.0 kDa
Protein length: 149 aaBLASTSequence
Gene length: 447 bpBLASTSequenceSequence + Flanks
Function: transcriptional regulator of arginine metabolic genes
Product: transcriptional regulator (ArgR family)
Essential: no
E.C. number:
Synonyms: argR
Databases: SubtiListKEGGUniProtExpression data browser

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, glutamate metabolism, utilization of amino acids, transcription factors and their control

This gene is a member of the following regulons

SR1 regulon

The AhrC regulon


  • Coordinates on the chromosome (coding sequence): 2,522,324 -> 2,522,773
  • The protein

    Catalyzed reaction/ biological activity

  • transcriptional activator/ repressor of genes involved in arginine metabolism
  • Protein family

  • ArgR family
  • Paralogous protein(s)

    Kinetic information




  • L-arginine is the co-factor required for transcription repression/ activation
  • Effectors of protein activity


  • 2P5M (C-Terminus), 2P5K (complex with an 18bp DNA operator), 2P5L (N-terminus), 1F9N, NCBI PubMed,N-Terminus NCBI, C-Terminus NCBI, complex with an 18bp DNA operator NCBI
  • Localization

  • Cytoplasm
  • Interactions

    Additional information

    Expression and Regulation


  • ahrC-recN PubMed
  • Sigma factor


  • by sRNA sr1
  • Regulatory mechanism

  • inhibtion of translation upon binding of sr1 to the ahrC mRNA PubMed
  • Additional information

  • expression is fourfold increased upon depletion of nusA Reference
  • Biological materials


  • GP729 (aphA3), available in Stülke lab
  • GP2185 (ahrC::ermC), available in Jörg Stülke's lab
  • Expression vector

    lacZ fusion

    GFP fusion

    two-hybrid system

    FLAG-tag construct


    Labs working on this gene/protein

  • Simon Phillips, Leeds University, UK Homepage
  • Michel Debarbouille, Pasteur Institute, Paris, France Homepage
  • References

    Park YW, Kang J, Yeo HK, Lee JY

    Structural Analysis and Insights into the Oligomeric State of an Arginine-Dependent Transcriptional Regulator from Bacillus halodurans

    PLoS One. 2016 May 12;11(5):e0155396. doi: 10.1371/journal.pone.0155396. eCollection 2016. PubMed PMID: 27171430; PubMed Central PMCID: PMC4865122.
    Garnett JA, Marincs F, Baumberg S, Stockley PG, Phillips SE

    Structure and function of the arginine repressor-operator complex from Bacillus subtilis

    J Mol Biol. 2008 May 30;379(2):284-98. doi: 10.1016/j.jmb.2008.03.007. Epub 2008 Mar 12. PubMed PMID: 18455186.
    Garnett JA, Baumberg S, Stockley PG, Phillips SE

    Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine

    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):918-21. Epub 2007 Oct 20. PubMed PMID: 18007040; PubMed Central PMCID: PMC2339756.
    Garnett JA, Baumberg S, Stockley PG, Phillips SE

    A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis

    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):914-7. Epub 2007 Oct 20. PubMed PMID: 18007039; PubMed Central PMCID: PMC2339755.
    Heidrich N, Moll I, Brantl S

    In vitro analysis of the interaction between the small RNA SR1 and its primary target ahrC mRNA

    Nucleic Acids Res. 2007;35(13):4331-46. Epub 2007 Jun 18. PubMed PMID: 17576690; PubMed Central PMCID: PMC1935000.
    Heidrich N, Chinali A, Gerth U, Brantl S

    The small untranslated RNA SR1 from the Bacillus subtilis genome is involved in the regulation of arginine catabolism

    Mol Microbiol. 2006 Oct;62(2):520-36. PubMed PMID: 17020585.
    Dennis C CA, Glykos NM, Parsons MR, Phillips SE

    The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis

    Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):421-30. Epub 2002 Feb 21. PubMed PMID: 11856827.
    Makarova KS, Mironov AA, Gelfand MS

    Conservation of the binding site for the arginine repressor in all bacterial lineages

    Genome Biol. 2001;2(4):RESEARCH0013. Epub 2001 Mar 22. PubMed PMID: 11305941; PubMed Central PMCID: PMC31482.
    Miller CM, Baumberg S, Stockley PG

    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. 1997 Oct;26(1):37-48. PubMed PMID: 9383188.
    Klingel U, Miller CM, North AK, Stockley PG, Baumberg S

    A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/activator of arginine metabolism

    Mol Gen Genet. 1995 Aug 21;248(3):329-40. PubMed PMID: 7565595.
    Van Hoy BE, Hoch JA

    Characterization of the spoIVB and recN loci of Bacillus subtilis

    J Bacteriol. 1990 Mar;172(3):1306-11. PubMed PMID: 2106508; PubMed Central PMCID: PMC208599.
    Czaplewski LG, North AK, Smith MC, Baumberg S, Stockley PG

    Purification and initial characterization of AhrC: the regulator of arginine metabolism genes in Bacillus subtilis

    Mol Microbiol. 1992 Jan;6(2):267-75. PubMed PMID: 1312212.
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