Difference between revisions of "YhcR"
(→References) |
(→References) |
||
Line 130: | Line 130: | ||
=References= | =References= | ||
− | '''Additional referencecs:''' {{PubMed|21906378}} | + | '''Additional referencecs:''' {{PubMed|21906378,22020651}} |
− | <pubmed>15292138,21800427,18957862, | + | <pubmed>15292138,21800427,18957862, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 07:53, 26 October 2011
- Description: extracellular non-specific endonuclease, Rnase
Gene name | yhcR |
Synonyms | |
Essential | no |
Product | extracellular non-specific endonuclease, Rnase |
Function | utilization of nucleic acids |
Interactions involving this protein in SubtInteract: YhcR | |
MW, pI | 132 kDa, 4.693 |
Gene length, protein length | 3651 bp, 1217 aa |
Immediate neighbours | yhcQ, yhcS |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of nucleotides, Rnases
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU09190
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s): YfkN
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions: YhcS-YhcR PubMed (anchoring to the cell wall)
- Localization: extracellular (signal peptide) PubMed, attached to the cell wall PubMed
Database entries
- Structure:
- UniProt: P54602
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
David Bechhofer, Mount Sinai School, New York, USA Homepage
Your additional remarks
References
Additional referencecs: PubMed
Hamidreza Fasehee, Helga Westers, Albert Bolhuis, Haike Antelmann, Michael Hecker, Wim J Quax, Agha F Mirlohi, Jan Maareten van Dijl, Gholamreza Ahmadian
Functional analysis of the sortase YhcS in Bacillus subtilis.
Proteomics: 2011, 11(19);3905-13
[PubMed:21800427]
[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)
Irina A Oussenko, Roberto Sanchez, David H Bechhofer
Bacillus subtilis YhcR, a high-molecular-weight, nonspecific endonuclease with a unique domain structure.
J Bacteriol: 2004, 186(16);5376-83
[PubMed:15292138]
[WorldCat.org]
[DOI]
(P p)