Difference between revisions of "BslA"
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− | <pubmed> 22607588 </pubmed> | + | <pubmed> 22607588 23979433 </pubmed> |
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==Original publications== | ==Original publications== | ||
<pubmed> 22571672 18978066 18957862 17850253 21097620 21742882 22383849 23335417 23904481 22571672 </pubmed> | <pubmed> 22571672 18978066 18957862 17850253 21097620 21742882 22383849 23335417 23904481 22571672 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 15:37, 28 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biofilm formation, phosphorelay
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31080
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Protein family:
- Paralogous protein(s): SivA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P71014
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- 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:
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)