BslA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• BsubCyc: BSU31080

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • inhibits KinA autophophorylation PubMed

• Protein family:

• Paralogous protein(s): SivA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • extracellular (signal peptide) PubMed
  • biofilm matrix in an extracellular polysaccharide-dependent manner PubMed
  • forms a layer on the biofilm surface PubMed

Database entries

• BsubCyc: BSU31080

• Structure:
  • 4BHU PubMed

• UniProt: P71014

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: bslA PubMed

• Expression browser: yuaB PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:
  • AbrB: transcription repression PubMed
  • LutR: transcription activation PubMed
  • expression is down-regulated in a rok mutant (indirect effect) PubMed
  • DegU-P: transcription activation PubMed, this might be indirect PubMed

• Additional information:

Biological materials

• Mutant:
  • B. subtilis W939 bslA::Cm (ATCC6051 based) PubMed
  • B. subtilis NRS2097 bslA::Cm (NCIB3610 based) PubMed
  • B. subtilis bslA::Cm (168 based) PubMed

• Expression vector:
  • Physpank-bslA based on vector pDR111: pDRyuaB2 PubMed

• lacZ fusion:
  • pNW500 PbslA-lacZ fusion in pDG1663 PubMed

• GFP fusion:
  • PbslA-gfp fusion in pSG1151 vector: pSGyuaB PubMed

• two-hybrid system:

• Antibody:

References

Original publications

Keith M Bromley, Ryan J Morris, Laura Hobley, Giovanni Brandani, Rachel M C Gillespie, Matthew McCluskey, Ulrich Zachariae, Davide Marenduzzo, Nicola R Stanley-Wall, Cait E MacPhee
Interfacial self-assembly of a bacterial hydrophobin.
Proc Natl Acad Sci U S A: 2015, 112(17);5419-24
[PubMed:25870300] [WorldCat.org] [DOI] (I p)

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)