Difference between revisions of "SivA"

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* the'' [[sivA]] [[bslA]]'' double mutant exhibits a more severe loss of repellency of the biofilm surface as compared to the ''[[bslA]]'' mutant {{PubMed|22571672}}  
 
* the'' [[sivA]] [[bslA]]'' double mutant exhibits a more severe loss of repellency of the biofilm surface as compared to the ''[[bslA]]'' mutant {{PubMed|22571672}}  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37800&redirect=T BSU37800]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yweA.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yweA.html]
Line 89: Line 90:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37800&redirect=T BSU37800]
  
 
* '''Structure:'''
 
* '''Structure:'''

Latest revision as of 15:06, 2 April 2014

  • Description: inhibitor of KinA autophosphorylation, and subsequently of entry into sporulation

Gene name yweA
Synonyms ipa-74d
Essential no
Product inhibitor of KinA autophosphorylation
Function control of entry into sporulation via the phosphorelay
Gene expression levels in SubtiExpress: sivA
MW, pI 16 kDa, 7.175
Gene length, protein length 462 bp, 154 aa
Immediate neighbours rocG, spsL
Sequences Protein DNA DNA_with_flanks
Genetic context
YweA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YweA expression.png















Categories containing this gene/protein

phosphorelay

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

  • Locus tag: BSU37800

Phenotypes of a mutant

  • the sivA bslA double mutant exhibits a more severe loss of repellency of the biofilm surface as compared to the bslA mutant PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

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

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

  • Regulation:
  • Regulatory mechanism:
  • 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

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)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [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)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)