Difference between revisions of "Prs"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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=== Additional information===
 
=== Additional information===
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''  
 
* '''Effectors of protein activity:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=prs_57745_58698_1 prs] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=prs_57745_58698_1 prs] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/pubmed/8522540 PubMed]
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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/pubmed/8522540 PubMed]
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
'''Additional publications:''' {{PubMed|22083279}}
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<pubmed>12837783,2169413,8522540, 19446032, 12837783, 12837784, 19446032 22083279</pubmed>
<pubmed>12837783,2169413,8522540, 19446032, 12837783, 12837784, 19446032</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:29, 14 March 2014

Gene name prs
Synonyms
Essential yes PubMed
Product phosphoribosylpyrophosphate synthetase
Function phosphoribosylpyrophosphate synthesis
(biosynthesis of histidine)
Gene expression levels in SubtiExpress: prs
Interactions involving this protein in SubtInteract: Prs
Metabolic function and regulation of this protein in SubtiPathways:
prs
MW, pI 34 kDa, 5.895
Gene length, protein length 951 bp, 317 aa
Immediate neighbours gcaD, ctc
Sequences Protein DNA DNA_with_flanks
Genetic context
Prs context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Prs expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, biosynthesis/ acquisition of nucleotides, essential genes, universally conserved proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU00510

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate (according to Swiss-Prot)
  • Protein family: ribose-phosphate pyrophosphokinase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
    • subject to feedback inhibition by two end products of purine biosynthesis, adenosine 5'-diphosphate (ADP) and guanosine 5'-diphosphate (GDP) PubMed

Database entries

  • KEGG entry: [3]

Additional information

universally conserved protein

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Natalia P Zakataeva, Dmitriy V Romanenkov, Victoria S Skripnikova, Maria V Vitushkina, Vitaliy A Livshits, Alexandr D Kivero, Anna E Novikova
Wild-type and feedback-resistant phosphoribosyl pyrophosphate synthetases from Bacillus amyloliquefaciens: purification, characterization, and application to increase purine nucleoside production.
Appl. Microbiol. Biotechnol.: 2012, 93(5);2023-33
[PubMed:22083279] [WorldCat.org] [DOI] (I p)

Shuobo Shi, Tao Chen, Zhigang Zhang, Xun Chen, Xueming Zhao
Transcriptome analysis guided metabolic engineering of Bacillus subtilis for riboflavin production.
Metab. Eng.: 2008, 11(4-5);243-52
[PubMed:19446032] [WorldCat.org] [DOI] (I p)

Aloke Kumar Bera, Jianghai Zhu, Howard Zalkin, Janet L Smith
Functional dissection of the Bacillus subtilis pur operator site.
J. Bacteriol.: 2003, 185(14);4099-109
[PubMed:12837784] [WorldCat.org] [DOI] (P p)

Sangita C Sinha, Joseph Krahn, Byung Sik Shin, Diana R Tomchick, Howard Zalkin, Janet L Smith
The purine repressor of Bacillus subtilis: a novel combination of domains adapted for transcription regulation.
J. Bacteriol.: 2003, 185(14);4087-98
[PubMed:12837783] [WorldCat.org] [DOI] (P p)

I Hilden, B N Krath, B Hove-Jensen
Tricistronic operon expression of the genes gcaD (tms), which encodes N-acetylglucosamine 1-phosphate uridyltransferase, prs, which encodes phosphoribosyl diphosphate synthetase, and ctc in vegetative cells of Bacillus subtilis.
J. Bacteriol.: 1995, 177(24);7280-4
[PubMed:8522540] [WorldCat.org] [DOI] (P p)

K Arnvig, B Hove-Jensen, R L Switzer
Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis.
Eur. J. Biochem.: 1990, 192(1);195-200
[PubMed:2169413] [WorldCat.org] [DOI] (P p)