Difference between revisions of "YvmC"
Line 95: | Line 95: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
+ | ** [[AbrB]]: transcription repression {{PubMed|20817675}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
Line 117: | Line 118: | ||
=References= | =References= | ||
− | <pubmed> 19430487 4204912 </pubmed> | + | <pubmed> 19430487 4204912 20817675</pubmed> |
[http://www.liebertonline.com/doi/pdf/10.1089/ind.2006.2.66 additional paper] | [http://www.liebertonline.com/doi/pdf/10.1089/ind.2006.2.66 additional paper] | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 20:40, 15 September 2010
- Description: cyclodipeptide synthase
Gene name | yvmC |
Synonyms | |
Essential | no |
Product | cyclodipeptide synthase |
Function | biosynthesis of the extracellular iron chelate pulcherrimin |
MW, pI | 28 kDa, 6.612 |
Gene length, protein length | 744 bp, 248 aa |
Immediate neighbours | cypX, yvmB |
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: BSU35070
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- synthesis of the cyclic dipeptide cyclo-L-leucyl-L-leucyl with the corresponding charged tRNAs as substrates in an ATP-dependent manner PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: O34351
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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)
Muriel Gondry, Ludovic Sauguet, Pascal Belin, Robert Thai, Rachel Amouroux, Carine Tellier, Karine Tuphile, Mickaël Jacquet, Sandrine Braud, Marie Courçon, Cédric Masson, Steven Dubois, Sylvie Lautru, Alain Lecoq, Shin-ichi Hashimoto, Roger Genet, Jean-Luc Pernodet
Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes.
Nat Chem Biol: 2009, 5(6);414-20
[PubMed:19430487]
[WorldCat.org]
[DOI]
(I p)
R L Uffen, E Canale-Parola
Synthesis of pulcherriminic acid by Bacillus subtilis.
J Bacteriol: 1972, 111(1);86-93
[PubMed:4204912]
[WorldCat.org]
[DOI]
(P p)