Difference between revisions of "YurI"
| Line 97: | Line 97: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
** [[PhoP]]: transcription activation {{PubMed|16291680}} | ** [[PhoP]]: transcription activation {{PubMed|16291680}} | ||
| + | ** [[AbrB]]: transcription repression {{PubMed|20817675}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
| Line 120: | Line 121: | ||
=References= | =References= | ||
| − | <pubmed>16291680,18957862, 12490701 1396690 20709850 </pubmed> | + | <pubmed>16291680,18957862, 12490701 1396690 20709850 20817675</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 20:16, 15 September 2010
- 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 
This image was kindly provided by SubtiList
| |
Contents
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:
- UniProt: O32150
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: yurI 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
Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675]
[WorldCat.org]
[DOI]
(I p)
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)
