Difference between revisions of "BslA"

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(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' ** [http://www.rcsb.org/pdb/explore.do?structureId=4BHU 4BHU] {{PubMed|23904481}}
+
* '''Structure:'''
 +
** [http://www.rcsb.org/pdb/explore.do?structureId=4BHU 4BHU] {{PubMed|23904481}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P71014 P71014]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P71014 P71014]

Revision as of 07:57, 2 August 2013

  • Description: bacterial hydrophobin, forms water-repellent surface layer of the biofilm, inhibitor of KinA autophosphorylation, and subsequently of entry into sporulation

Gene name bslA
Synonyms yuaB, sivB
Essential no
Product biofilm surface layer, inhibitor of KinA autophosphorylation
Function biofilm formation, control of entry into sporulation via the phosphorelay
Gene expression levels in SubtiExpress: bslA
MW, pI 19 kDa, 9.987
Gene length, protein length 543 bp, 181 aa
Immediate neighbours gbsR, ktrA
Sequences Protein DNA DNA_with_flanks
Genetic context
YuaB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YuaB expression.png















Categories containing this gene/protein

biofilm formation, phosphorelay

This gene is a member of the following regulons

AbrB regulon, DegU regulon

The gene

Basic information

  • Locus tag: BSU31080

Phenotypes of a mutant

  • reduced colony complexity PubMed
  • loss of surface repellency of the biofilm PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s): SivA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • extracellular (signal peptide) PubMed
    • biofilm matrix in an extracellular polysaccharide-dependent manner PubMed
    • forms a layer on the biofilm surface PubMed

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • expression is down-regulated in a rok mutant (indirect effect) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
    • B. subtilis W939 yuaB::Cm (ATCC6051 based) PubMed
    • B. subtilis NRS2097 yuaB::Cm (NCIB3610 based) PubMed
    • B. subtilis yuaB::Cm (168 based) PubMed
  • Expression vector:
    • Physpank-yuaB based on vector pDR111: pDRyuaB2 PubMed
  • lacZ fusion:
    • pNW500 PyuaB-lacZ fusion in pDG1663 PubMed
  • GFP fusion:
    • PyuaB-gfp fusion in pSG1151 vector: pSGyuaB PubMed
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Laura Hobley, Adam Ostrowski, Francesco V Rao, Keith M Bromley, Michael Porter, Alan R Prescott, Cait E MacPhee, Daan M F van Aalten, Nicola R Stanley-Wall
BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.
Proc Natl Acad Sci U S A: 2013, 110(33);13600-5
[PubMed:23904481] [WorldCat.org] [DOI] (I p)

Sharon Garti-Levi, Ashlee Eswara, Yoav Smith, Masaya Fujita, Sigal Ben-Yehuda
Novel modulators controlling entry into sporulation in Bacillus subtilis.
J Bacteriol: 2013, 195(7);1475-83
[PubMed:23335417] [WorldCat.org] [DOI] (I p)

Kazuo Kobayashi, Megumi Iwano
BslA(YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis biofilms.
Mol Microbiol: 2012, 85(1);51-66
[PubMed:22571672] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Adam Ostrowski, Angela Mehert, Alan Prescott, Taryn B Kiley, Nicola R Stanley-Wall
YuaB functions synergistically with the exopolysaccharide and TasA amyloid fibers to allow biofilm formation by Bacillus subtilis.
J Bacteriol: 2011, 193(18);4821-31
[PubMed:21742882] [WorldCat.org] [DOI] (I p)

Akos T Kovács, Oscar P Kuipers
Rok regulates yuaB expression during architecturally complex colony development of Bacillus subtilis 168.
J Bacteriol: 2011, 193(4);998-1002
[PubMed:21097620] [WorldCat.org] [DOI] (I p)

Daniel T Verhamme, Ewan J Murray, Nicola R Stanley-Wall
DegU and Spo0A jointly control transcription of two loci required for complex colony development by Bacillus subtilis.
J Bacteriol: 2009, 191(1);100-8
[PubMed:18978066] [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)

Kazuo Kobayashi
Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2007, 66(2);395-409
[PubMed:17850253] [WorldCat.org] [DOI] (P p)