PyrR

• Description: transcriptional antiterminator of the pyr operon
  
  

Gene name	pyrR
Synonyms
Essential	no
Product	transcriptional antiterminator with minor uracil phosphoribosyltransferase activity
Function	regulation of pyrimidine biosynthesis
MW, pI	20 kDa, 4.991
Gene length, protein length	543 bp, 181 aa
Immediate neighbours	ylyB, pyrP
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: BSU15470

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate (according to Swiss-Prot)

• Protein family: PyrR subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: PyrR-PyrR

• Localization:

Database entries

• Structure: 1A3C (dimeric form)

• Swiss prot entry: P39765

• KEGG entry: [3]

• E.C. number: 2.4.2.9

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:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

D R Tomchick, R J Turner, R L Switzer, J L Smith
Adaptation of an enzyme to regulatory function: structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase.
Structure: 1998, 6(3);337-50
[PubMed:9551555] [WorldCat.org] [DOI] (P p)

R J Turner, E R Bonner, G K Grabner, R L Switzer
Purification and characterization of Bacillus subtilis PyrR, a bifunctional pyr mRNA-binding attenuation protein/uracil phosphoribosyltransferase.
J Biol Chem: 1998, 273(10);5932-8
[PubMed:9488732] [WorldCat.org] [DOI] (P p)

1. Tomchik, D. R., Turner, R. J., Switzer, R. L., and Smith, J. L. (1998) Adaptation of an enzyme to regulatory function: structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase. Structure 6: 337-350. PubMed
2. Turner, R. J., Bonner, E. R., Grabner, G. K., and Switzer, R. L. (1998) Purification and characterization of Bacillus subtilis PyrR, a bifunctional pyr mRNA-binding attenuation protein/uracil phosphoribosyltransferase. J Biol Chem 273: 5932-5938. PubMed
3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed