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

Preethi Chander, Kari M Halbig, Jamie K Miller, Christopher J Fields, Heather K S Bonner, Gail K Grabner, Robert L Switzer, Janet L Smith
Structure of the nucleotide complex of PyrR, the pyr attenuation protein from Bacillus caldolyticus, suggests dual regulation by pyrimidine and purine nucleotides.
J Bacteriol: 2005, 187(5);1773-82
[PubMed:15716449] [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)

Gail K Grabner, Robert L Switzer
Kinetic studies of the uracil phosphoribosyltransferase reaction catalyzed by the Bacillus subtilis pyrimidine attenuation regulatory protein PyrR.
J Biol Chem: 2003, 278(9);6921-7
[PubMed:12482852] [WorldCat.org] [DOI] (P p)

Heather K Savacool, Robert L Switzer
Characterization of the interaction of Bacillus subtilis PyrR with pyr mRNA by site-directed mutagenesis of the protein.
J Bacteriol: 2002, 184(9);2521-8
[PubMed:11948166] [WorldCat.org] [DOI] (P p)

E R Bonner, J N D'Elia, B K Billips, R L Switzer
Molecular recognition of pyr mRNA by the Bacillus subtilis attenuation regulatory protein PyrR.
Nucleic Acids Res: 2001, 29(23);4851-65
[PubMed:11726695] [WorldCat.org] [DOI] (I p)

R L Switzer, R J Turner, Y Lu
Regulation of the Bacillus subtilis pyrimidine biosynthetic operon by transcriptional attenuation: control of gene expression by an mRNA-binding protein.
Prog Nucleic Acid Res Mol Biol: 1999, 62;329-67
[PubMed:9932459] [WorldCat.org] [DOI] (P p)

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)

Y Lu, R L Switzer
Transcriptional attenuation of the Bacillus subtilis pyr operon by the PyrR regulatory protein and uridine nucleotides in vitro.
J Bacteriol: 1996, 178(24);7206-11
[PubMed:8955403] [WorldCat.org] [DOI] (P p)

Y Lu, R L Switzer
Evidence that the Bacillus subtilis pyrimidine regulatory protein PyrR acts by binding to pyr mRNA at three sites in vivo.
J Bacteriol: 1996, 178(19);5806-9
[PubMed:8824632] [WorldCat.org] [DOI] (P p)

A E Kahler, R L Switzer
Identification of a novel gene of pyrimidine nucleotide biosynthesis, pyrDII, that is required for dihydroorotate dehydrogenase activity in Bacillus subtilis.
J Bacteriol: 1996, 178(16);5013-6
[PubMed:8759868] [WorldCat.org] [DOI] (P p)

S Y Ghim, R L Switzer
Mutations in Bacillus subtilis PyrR, the pyr regulatory protein, with defects in regulation by pyrimidines.
FEMS Microbiol Lett: 1996, 137(1);13-8
[PubMed:8935652] [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)

J Martinussen, P Glaser, P S Andersen, H H Saxild
Two genes encoding uracil phosphoribosyltransferase are present in Bacillus subtilis.
J Bacteriol: 1995, 177(1);271-4
[PubMed:7798145] [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)