Difference between revisions of "ArgG"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[argH]]'', ''[[moaB]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[argH]]'', ''[[moaB]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU29450 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU29450 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU29450 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU29450 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU29450 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU29450 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:argG_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:argG_context.gif]]

Revision as of 11:00, 14 May 2013

  • Description: argininosuccinate synthase, reversible

Gene name argG
Synonyms
Essential no
Product argininosuccinate synthase, reversible
Function biosynthesis of arginine
Gene expression levels in SubtiExpress: argG
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
Sequences Protein DNA DNA_with_flanks
Genetic context
ArgG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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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

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

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:

Database entries

  • Structure: 1KH1 (from Thermus thermophilus, 44% identity, 65% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • 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:

Labs working on this gene/protein

Your additional remarks

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)