RocF

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  • Description: arginase

Gene name rocF
Synonyms
Essential no
Product arginase
Function arginine utilization
Gene expression levels in SubtiExpress: rocF
Metabolic function and regulation of this protein in SubtiPathways:
Ammonium/ glutamate
MW, pI 32 kDa, 4.932
Gene length, protein length 888 bp, 296 aa
Immediate neighbours phrG, rocE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RocF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RocF expression.png















Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

AhrC regulon, CodY regulon, RocR regulon, SigL regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU40320

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-arginine + H2O = L-ornithine + urea (according to Swiss-Prot)
  • Protein family: arginase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on Ser-68 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2EF5 (from Thermus thermophilus, 46% identity, 63% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induced by arginine (RocR, AhrC) PubMed
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Additional information:

Biological materials

  • Mutant: GP655, aphA3, available in the Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Jin-Ju Yu, Ki-Bum Park, Su-Gon Kim, Suk-Heung Oh
Expression, purification, and biochemical properties of arginase from Bacillus subtilis 168.
J Microbiol: 2013, 51(2);222-8
[PubMed:23625224] [WorldCat.org] [DOI] (I p)

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

R Gardan, G Rapoport, M Débarbouillé
Expression of the rocDEF operon involved in arginine catabolism in Bacillus subtilis.
J Mol Biol: 1995, 249(5);843-56
[PubMed:7540694] [WorldCat.org] [DOI] (P p)