Difference between revisions of "CshB"
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Revision as of 13:56, 16 May 2013
- Description: DEAD-box RNA helicase, important for adaptation to low temperatures
Gene name | cshB |
Synonyms | yqfR |
Essential | no |
Product | DEAD-box RNA helicase |
Function | RNA helicase |
Gene expression levels in SubtiExpress: cshB | |
Interactions involving this protein in SubtInteract: CshB | |
MW, pI | 49 kDa, 9.89 |
Gene length, protein length | 1314 bp, 438 aa |
Immediate neighbours | nfo, yqfQ |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
DEAD-box RNA helicases, translation
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU25140
Phenotypes of a mutant
- poor growth at low temperatures (16 to 20°C) PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Protein family: 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:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- GP1051 (cat), available in Jörg Stülke's lab
- Expression vector:
- for expression/ purification from B. subtilis with C-terminal Strep-tag, for SPINE, expression from the native chromomsomal site: GP1064 (spc), available in Jörg Stülke's lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- FLAG-tag construct:
- GP1011 (spc, based on pGP1331), available in Jörg Stülke's lab
- Antibody:
Labs working on this gene/protein
Mohamed Marahiel, Marburg University, Germany homepage
Your additional remarks
References
Additional publications: PubMed