TasA

From SubtiWiki
Revision as of 10:07, 1 February 2013 by Jstuelk (talk | contribs) (Original publications)
Jump to: navigation, search
  • 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
TasA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TasA expression.png















Categories containing this gene/protein

biofilm formation

This gene is a member of the following regulons

AbrB regulon, SinR regulon

The gene

Basic information

  • Locus tag: BSU24620

Phenotypes of a mutant

  • altered cell death pattern in colonies PubMed

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:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and 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

Reviews


Original publications

Additional publications: PubMed

Diego Romero, Edgardo Sanabria-Valentín, Hera Vlamakis, Roberto Kolter
Biofilm inhibitors that target amyloid proteins.
Chem Biol: 2013, 20(1);102-10
[PubMed:23352144] [WorldCat.org] [DOI] (I p)

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