Difference between revisions of "YurI"

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(This gene is a member of the following regulons)
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* '''Operon:''' ''yurI'' {{PubMed|16291680}}
 
* '''Operon:''' ''yurI'' {{PubMed|16291680}}
  
* '''[[Sigma factor]]:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bsn_3344113_3344979_1 yurI] {{PubMed|22383849}}
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* '''Sigma factor:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 16:46, 16 April 2012

  • Description: ribonuclease, extracellular RNase Bsn

Gene name yurI
Synonyms
Essential no
Product extracellular RNase Bsn
Function extracellular RNA degradation
MW, pI 31 kDa, 4.87
Gene length, protein length 864 bp, 288 aa
Immediate neighbours pucF, yurJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YurI context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

phosphate metabolism, Rnases

This gene is a member of the following regulons

AbrB regulon, PhoP regulon

The gene

Basic information

  • Locus tag: BSU32540

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: extracellular (signal peptide) PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • expressed under conditions of phosphate limitation (PhoP) PubMed
  • 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

Additional publications: PubMed

Christian Degering, Thorsten Eggert, Michael Puls, Johannes Bongaerts, Stefan Evers, Karl-Heinz Maurer, Karl-Erich Jaeger
Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides.
Appl Environ Microbiol: 2010, 76(19);6370-6
[PubMed:20709850] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Nicholas E E Allenby, Nicola O'Connor, Zoltán Prágai, Alan C Ward, Anil Wipat, Colin R Harwood
Genome-wide transcriptional analysis of the phosphate starvation stimulon of Bacillus subtilis.
J Bacteriol: 2005, 187(23);8063-80
[PubMed:16291680] [WorldCat.org] [DOI] (P p)

Ciarán Condon, Harald Putzer
The phylogenetic distribution of bacterial ribonucleases.
Nucleic Acids Res: 2002, 30(24);5339-46
[PubMed:12490701] [WorldCat.org] [DOI] (I p)

A Nakamura, Y Koide, H Miyazaki, A Kitamura, H Masaki, T Beppu, T Uozumi
Gene cloning and characterization of a novel extracellular ribonuclease of Bacillus subtilis.
Eur J Biochem: 1992, 209(1);121-7
[PubMed:1396690] [WorldCat.org] [DOI] (P p)