AraR

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Gene name araR
Synonyms araC, yvbS
Essential no
Product transcriptional repressor (GntR family, LacI family)
Function regulation of arabinose utilization

(araABDLMNPQ-abfA) and of the araE/araR genes

Gene expression levels in SubtiExpress: araR

(araABDLMNPQ-abfA) and of the araE/araR genes

Metabolic function and regulation of this protein in SubtiPathways:
AraR
MW, pI 43 kDa, 6.341
Gene length, protein length 1152 bp, 384 aa
Immediate neighbours araE, yvbT
Sequences Protein DNA DNA_with_flanks
Genetic context
AraR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AraR expression.png















Categories containing this gene/protein

utilization of specific carbon sources, transcription factors and their control

This gene is a member of the following regulons

AraR regulon

The AraR regulon

The gene

Basic information

  • Locus tag: BSU33970

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Isabel Lopes Correia, Irina Saraiva Franco, Isabel de Sá-Nogueira
Towards novel amino acid-base contacts in gene regulatory proteins: AraR--a case study.
PLoS One: 2014, 9(11);e111802
[PubMed:25364981] [WorldCat.org] [DOI] (I e)

Deepti Jain, Deepak T Nair
Spacing between core recognition motifs determines relative orientation of AraR monomers on bipartite operators.
Nucleic Acids Res: 2013, 41(1);639-47
[PubMed:23109551] [WorldCat.org] [DOI] (I p)

Kateřina Procházková, Kateřina Cermáková, Petr Pachl, Irena Sieglová, Milan Fábry, Zbyszek Otwinowski, Pavlína Rezáčová
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis.
Acta Crystallogr D Biol Crystallogr: 2012, 68(Pt 2);176-85
[PubMed:22281747] [WorldCat.org] [DOI] (I p)

Irina Saraiva Franco, Luís Jaime Mota, Cláudio Manuel Soares, Isabel de Sá-Nogueira
Probing key DNA contacts in AraR-mediated transcriptional repression of the Bacillus subtilis arabinose regulon.
Nucleic Acids Res: 2007, 35(14);4755-66
[PubMed:17617643] [WorldCat.org] [DOI] (I p)

Irina Saraiva Franco, Luís Jaime Mota, Cláudio Manuel Soares, Isabel de Sá-Nogueira
Functional domains of the Bacillus subtilis transcription factor AraR and identification of amino acids important for nucleoprotein complex assembly and effector binding.
J Bacteriol: 2006, 188(8);3024-36
[PubMed:16585763] [WorldCat.org] [DOI] (P p)

Maria Paiva Raposo, José Manuel Inácio, Luís Jaime Mota, Isabel de Sá-Nogueira
Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis.
J Bacteriol: 2004, 186(5);1287-96
[PubMed:14973026] [WorldCat.org] [DOI] (P p)

L J Mota, L M Sarmento, I de Sá-Nogueira
Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: crucial roles of operators, cooperativity, and DNA looping.
J Bacteriol: 2001, 183(14);4190-201
[PubMed:11418559] [WorldCat.org] [DOI] (P p)

L J Mota, P Tavares, I Sá-Nogueira
Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis.
Mol Microbiol: 1999, 33(3);476-89
[PubMed:10417639] [WorldCat.org] [DOI] (P p)

I Sá-Nogueira, L J Mota
Negative regulation of L-arabinose metabolism in Bacillus subtilis: characterization of the araR (araC) gene.
J Bacteriol: 1997, 179(5);1598-608
[PubMed:9045819] [WorldCat.org] [DOI] (P p)

I Sá-Nogueira, H Paveia, H de Lencastre
Isolation of constitutive mutants for L-arabinose utilization in Bacillus subtilis.
J Bacteriol: 1988, 170(6);2855-7
[PubMed:3131313] [WorldCat.org] [DOI] (P p)