PyrB

• Description: aspartate carbamoyltransferase
  
  

Gene name	pyrB
Synonyms
Essential	no
Product	aspartate carbamoyltransferase
Function	pyrimidine biosynthesis
MW, pI	34 kDa, 5.341
Gene length, protein length	912 bp, 304 aa
Immediate neighbours	pyrP, pyrC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU15490

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate (according to Swiss-Prot)

• Protein family: ATCase/OTCase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on Ser-303 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2AT2

• Swiss prot entry: P05654

• KEGG entry: [3]

• E.C. number: 2.1.3.2

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: pyrR-pyrP-pyrB-pyrC-pyrAA-pyrAB-pyrK-pyrD-pyrF-pyrE PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced in the absence of uridine nucleotides (PyrR) PubMed

• Regulatory mechanism:
  • PyrR: RNA switch, transcription termination/ antitermination (in the presence of uridine nucleotides: termination, in their absence: antitermination) PubMed

• Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

1. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
2. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed