Difference between revisions of "TasA"
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* '''Mutant:''' | * '''Mutant:''' | ||
+ | ** 1S121 ( ''tasA''::''spec''), {{PubMed|10049401}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S121&Search=1S121 BGSC] | ||
* '''Expression vector:''' | * '''Expression vector:''' |
Revision as of 12:26, 19 September 2012
- Description: major component of biofilm matrix, forms amyloid fibers
Gene name | tasA |
Synonyms | cotN, yqhF |
Essential | no |
Product | major component of biofilm matrix |
Function | biofilm formation |
Gene expression levels in SubtiExpress: tasA | |
Interactions involving this protein in SubtInteract: TasA | |
Regulation of this protein in SubtiPathways: Biofilm, Protein secretion | |
MW, pI | 28 kDa, 5.442 |
Gene length, protein length | 783 bp, 261 aa |
Immediate neighbours | sinR, sipW |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU24620
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: forms amyloid fibers that bind cells together in the biofilm PubMed
- Protein family: peptidase M73 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P54507
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947
Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J A Novel Factor Controlling Bistability in Bacillus subtilis: The YmdB Protein Affects Flagellin Expression and Biofilm Formation. J Bacteriol.: 2011, 193(21):5997-6007. PubMed:21856853