PyrB

• Description: aspartate carbamoyltransferase
  
  

Gene name	pyrB
Synonyms
Essential	no
Product	aspartate carbamoyltransferase
Function	pyrimidine biosynthesis
Gene expression levels in SubtiExpress: pyrB
Metabolic function and regulation of this protein in SubtiPathways: Pyrimidines, Nucleotides (regulation)
MW, pI	34 kDa, 5.341
Gene length, protein length	912 bp, 304 aa
Immediate neighbours	pyrP, pyrC
Sequences	Protein DNA Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, phosphoproteins

This gene is a member of the following regulons

PyrR regulon

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: 3R7D PubMed

• UniProt: 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

• Expression browser: pyrB 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

Katharine M Harris, Gregory M Cockrell, David E Puleo, Evan R Kantrowitz
Crystallographic snapshots of the complete catalytic cycle of the unregulated aspartate transcarbamoylase from Bacillus subtilis.
J Mol Biol: 2011, 411(1);190-200
[PubMed:21663747] [WorldCat.org] [DOI] (I p)

Birgit Hobl, Matthias Mack
The regulator protein PyrR of Bacillus subtilis specifically interacts in vivo with three untranslated regions within pyr mRNA of pyrimidine biosynthesis.
Microbiology (Reading): 2007, 153(Pt 3);693-700
[PubMed:17322189] [WorldCat.org] [DOI] (P p)

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)

Hesheng Zhang, Robert L Switzer
Transcriptional pausing in the Bacillus subtilis pyr operon in vitro: a role in transcriptional attenuation?
J Bacteriol: 2003, 185(16);4764-71
[PubMed:12896995] [WorldCat.org] [DOI] (P p)

Y Lu, R J Turner, R L Switzer
Roles of the three transcriptional attenuators of the Bacillus subtilis pyrimidine biosynthetic operon in the regulation of its expression.
J Bacteriol: 1995, 177(5);1315-25
[PubMed:7868607] [WorldCat.org] [DOI] (P p)

P Hu, R L Switzer
Evidence for substrate stabilization in regulation of the degradation of Bacillus subtilis aspartate transcarbamylase in vivo.
Arch Biochem Biophys: 1995, 316(1);260-6
[PubMed:7840626] [WorldCat.org] [DOI] (P p)

R J Turner, Y Lu, R L Switzer
Regulation of the Bacillus subtilis pyrimidine biosynthetic (pyr) gene cluster by an autogenous transcriptional attenuation mechanism.
J Bacteriol: 1994, 176(12);3708-22
[PubMed:8206849] [WorldCat.org] [DOI] (P p)

C L Quinn, B T Stephenson, R L Switzer
Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon.
J Biol Chem: 1991, 266(14);9113-27
[PubMed:1709162] [WorldCat.org] (P p)

C G Lerner, R L Switzer
Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB).
J Biol Chem: 1986, 261(24);11156-65
[PubMed:3015959] [WorldCat.org] (P p)

J S Brabson, M R Maurizi, R L Switzer
Aspartate transcarbamylase from Bacillus subtilis.
Methods Enzymol: 1985, 113;627-35
[PubMed:3937019] [WorldCat.org] [DOI] (P p)

R W Bond, R L Switzer
Degradation of aspartate transcarbamylase in Bacillus subtilis is deficient in rel mutants but is not mediated by guanosine polyphosphates.
J Bacteriol: 1984, 158(2);746-8
[PubMed:6427186] [WorldCat.org] [DOI] (P p)