Difference between revisions of "ThiC"

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=== Additional information===
 
=== Additional information===
  
:* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
+
* subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}}
 +
 
 
=Expression and regulation=
 
=Expression and regulation=
* '''Operon:'''  
+
* '''Operon:''' ''[[thiC]]'' {{PubMed|22383849}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=thiC_955895_957667_1 thiC] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=thiC_955895_957667_1 thiC] {{PubMed|22383849}}
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** [[Thi-box]]: [[RNA switch]] {{PubMed|12376536}}
 
** [[Thi-box]]: [[RNA switch]] {{PubMed|12376536}}
  
* '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
+
* '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}}
  
 
=Biological materials =
 
=Biological materials =
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==Original publications==
 
==Original publications==
<pubmed>16291685 9370266 20509597 12376536 22517742</pubmed>
+
<pubmed>16291685 9370266 20509597 12376536 22517742 22383849</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:47, 21 April 2012

  • Description: biosynthesis of the pyrimidine moiety of thiamine

Gene name thiC
Synonyms thiA
Essential no
Product unknown
Function biosynthesis of thiamine
Metabolic function and regulation of this protein in SubtiPathways:
Thiamin
MW, pI 65 kDa, 5.262
Gene length, protein length 1770 bp, 590 aa
Immediate neighbours ygaJ, ygaK
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ThiC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ThiC expression.png




























Categories containing this gene/protein

biosynthesis of cofactors, phosphoproteins

This gene is a member of the following regulons

Thi-box

The gene

Basic information

  • Locus tag: BSU08790

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: thiC family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-556 PubMed
    • phosphorylated on Ser-565, Ser-586 and Tyr-589 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Sigma factor:
  • Regulation:
    • repressed by thiamine and 2-methyl-4-amino-5-hydroxymethylpyrimidine PubMed
    • repressed by thiamine (Thi-box) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews


Original publications

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)

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)

Ghislain Schyns, Sébastien Potot, Yi Geng, Teresa M Barbosa, Adriano Henriques, John B Perkins
Isolation and characterization of new thiamine-deregulated mutants of Bacillus subtilis.
J Bacteriol: 2005, 187(23);8127-36
[PubMed:16291685] [WorldCat.org] [DOI] (P p)

Dmitry A Rodionov, Alexey G Vitreschak, Andrey A Mironov, Mikhail S Gelfand
Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms.
J Biol Chem: 2002, 277(50);48949-59
[PubMed:12376536] [WorldCat.org] [DOI] (P p)

Y Zhang, T P Begley
Cloning, sequencing and regulation of thiA, a thiamin biosynthesis gene from Bacillus subtilis.
Gene: 1997, 198(1-2);73-82
[PubMed:9370266] [WorldCat.org] [DOI] (P p)