ArgG

• Description: argininosuccinate synthase, reversible
  
  

Gene name	argG
Synonyms
Essential	no
Product	argininosuccinate synthase, reversible
Function	biosynthesis of arginine
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate
MW, pI	44 kDa, 5.028
Gene length, protein length	1209 bp, 403 aa
Immediate neighbours	argH, moaB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed 500px

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, phosphoproteins

This gene is a member of the following regulons

AhrC regulon

The gene

Basic information

• Locus tag: BSU29450

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate (according to Swiss-Prot)

• Protein family: Type 1 subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • S-cysteinylation after diamide stress (C187) PubMed
  • phosphorylated on Arg-262 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1KH1 (from Thermus thermophilus, 44% identity, 65% similarity) PubMed

• UniProt: O34347

• KEGG entry: [2]

• E.C. number: 6.3.4.5

Expression and regulation

• Operon: argG-argH PubMed

• Expression browser: argG PubMed

• Sigma factor:

• Regulation:
  • repressed by casamino acids PubMed
  • repressed by arginine (AhrC)

• Regulatory mechanism:
  • AhrC: transcription repression

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)