Difference between revisions of "CshB"
Line 78: | Line 78: | ||
* '''Structure:''' | * '''Structure:''' | ||
− | * ''' | + | * '''UniProt:''' [http://www.uniprot.org/uniprot/P54475 P54475] |
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU25140] | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU25140] |
Revision as of 13:38, 20 July 2009
- Description: DEAD-box RNA helicase
Gene name | cshB |
Synonyms | yqfR |
Essential | no |
Product | DEAD-box RNA helicase |
Function | RNA helicase |
MW, pI | 49 kDa, 9.89 |
Gene length, protein length | 1314 bp, 438 aa |
Immediate neighbours | nfo, yqfQ |
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: BSU25140
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: RNA helicase
- Protein family: DEAD box helicase family (according to Swiss-Prot) DEAD-box RNA helicase
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasma, colocalizes with the ribosomes PubMed
Database entries
- Structure:
- UniProt: P54475
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Mohamed Marahiel, Marburg University, Germany homepage
Your additional remarks
References
Karen Hunger, Carsten L Beckering, Frank Wiegeshoff, Peter L Graumann, Mohamed A Marahiel
Cold-induced putative DEAD box RNA helicases CshA and CshB are essential for cold adaptation and interact with cold shock protein B in Bacillus subtilis.
J Bacteriol: 2006, 188(1);240-8
[PubMed:16352840]
[WorldCat.org]
[DOI]
(P p)