RocF

• 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: rocF
MW, pI	32 kDa, 4.932
Gene length, protein length	888 bp, 296 aa
Immediate neighbours	phrG, rocE
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2CEV (from Bacillus caldevelox, 71% identity) PubMed

• UniProt: P39138

• KEGG entry: [3]

• E.C. number: 3.5.3.1

Expression and regulation

• Operon: rocD-rocE-rocF PubMed

• Expression browser: rocF PubMed

• Sigma factor: SigL PubMed

• 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

• Regulatory mechanism:
  • RocR, AhrC: transcription activation PubMed
  • Spo0A: transcription repression PubMed
  • CodY: transcription repression PubMed

• Additional information:

Biological materials

• Mutant: GP655, aphA3, available in the Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

M C Bewley, P D Jeffrey, M L Patchett, Z F Kanyo, E N Baker
Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily.
Structure: 1999, 7(4);435-48
[PubMed:10196128] [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)