Difference between revisions of "TasA"

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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=tasA_2553081_2553866_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:tasA_expression.png|500px]]
 
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Revision as of 08:20, 20 April 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
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

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

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

Diego Romero, Claudio Aguilar, Richard Losick, Roberto Kolter
Amyloid fibers provide structural integrity to Bacillus subtilis biofilms.
Proc Natl Acad Sci U S A: 2010, 107(5);2230-4
[PubMed:20080671] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Kazuo Kobayashi
SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 69(6);1399-410
[PubMed:18647168] [WorldCat.org] [DOI] (I p)

Frances Chu, Daniel B Kearns, Anna McLoon, Yunrong Chai, Roberto Kolter, Richard Losick
A novel regulatory protein governing biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 68(5);1117-27
[PubMed:18430133] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568] [WorldCat.org] [DOI] (P p)

Mark A Strauch, Benjamin G Bobay, John Cavanagh, Fude Yao, Angelo Wilson, Yoann Le Breton
Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.
J Bacteriol: 2007, 189(21);7720-32
[PubMed:17720793] [WorldCat.org] [DOI] (P p)

Steven S Branda, Frances Chu, Daniel B Kearns, Richard Losick, Roberto Kolter
A major protein component of the Bacillus subtilis biofilm matrix.
Mol Microbiol: 2006, 59(4);1229-38
[PubMed:16430696] [WorldCat.org] [DOI] (P p)

Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

A G Stöver, A Driks
Regulation of synthesis of the Bacillus subtilis transition-phase, spore-associated antibacterial protein TasA.
J Bacteriol: 1999, 181(17);5476-81
[PubMed:10464223] [WorldCat.org] [DOI] (P p)

M Serrano, R Zilhão, E Ricca, A J Ozin, C P Moran, A O Henriques
A Bacillus subtilis secreted protein with a role in endospore coat assembly and function.
J Bacteriol: 1999, 181(12);3632-43
[PubMed:10368135] [WorldCat.org] [DOI] (P p)

A G Stöver, A Driks
Secretion, localization, and antibacterial activity of TasA, a Bacillus subtilis spore-associated protein.
J Bacteriol: 1999, 181(5);1664-72
[PubMed:10049401] [WorldCat.org] [DOI] (P p)