Difference between revisions of "RocF"

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* '''Additional information:'''
 
* '''Additional information:'''
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 126 {{PubMed|24696501}}
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** number of protein molecules per cell (complex medium with amino acids, without glucose): 13789 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:57, 17 April 2014

  • 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
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:
  • Modification: phosphorylated on Ser-68 PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 2CEV (from Bacillus caldevelox, 71% identity) PubMed
  • 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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 126 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 13789 PubMed

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)

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)