ThiC

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization:

Database entries

• Structure: 1G6C

• UniProt: P45740

• KEGG entry: [2]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon:

• Expression browser: thiC PubMed

• Sigma factor:

• Regulation:
  • repressed by thiamine and 2-methyl-4-amino-5-hydroxymethylpyrimidine PubMed
  • repressed by thiamine (Thi-box) PubMed

• Regulatory mechanism:
  • Thi-box: RNA switch 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:

References

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)

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)