Difference between revisions of "SivA"

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* '''Description:''' unknown <br/><br/>
+
* '''Description:''' inhibitor of [[KinA]] autophosphorylation, and subsequently of entry into [[sporulation]] <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' || unknown
+
|style="background:#ABCDEF;" align="center"| '''Product''' || inhibitor of [[KinA]] autophosphorylation
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || unknown
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of entry into [[sporulation]] via the [[phosphorelay]]
 +
|-
 +
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU37800 sivA]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 7.175   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 7.175   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[rocG]]'', ''[[spsL]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[rocG]]'', ''[[spsL]]''
 
|-
 
|-
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|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/yweA_nucleotide.txt    Gene sequence     (+200bp)  ]'''
+
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU37800 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU37800 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU37800 DNA_with_flanks]
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|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/yweA_protein.txt Protein sequence]'''
 
 
|-
 
|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yweA_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yweA_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 +
|-
 +
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yweA_3882191_3882655_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:yweA_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU37800]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/>
  
−
<br/><br/>
+
= [[Categories]] containing this gene/protein =
 +
{{SubtiWiki category|[[phosphorelay]]}}
 +
 
 +
= This gene is a member of the following [[regulons]] =
 +
{{SubtiWiki regulon|[[AbrB regulon]]}}
  
 
=The gene=
 
=The gene=
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=== Basic information ===
 
=== Basic information ===
  
−
* '''Coordinates:'''
+
* '''Locus tag:''' BSU37800
  
 
===Phenotypes of a mutant ===
 
===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|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]
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=== Additional information===
 
=== Additional information===
−
 
  
 
=The protein=
 
=The protein=
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* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
 +
** inhibits [[KinA]] autophophorylation {{PubMed|23335417}}
  
 
* '''Protein family:'''
 
* '''Protein family:'''
  
−
* '''Paralogous protein(s):'''
+
* '''Paralogous protein(s):''' [[BslA]]
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
−
* '''Interactions:'''
+
* '''[[SubtInteract|Interactions]]:'''
  
−
* '''Localization:''' extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
+
* '''[[Localization]]:'''
 +
** membrane (according to Swiss-Prot)
 +
** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37800&redirect=T BSU37800]
  
 
* '''Structure:'''
 
* '''Structure:'''
  
−
* '''Swiss prot entry:'''
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39632 P39632]
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU37800]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU37800]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''
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=Expression and regulation=
 
=Expression and regulation=
 +
* '''Operon:''' ''sivA'' {{PubMed|12823818}}
  
−
* '''Operon:'''  
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yweA_3882191_3882655_-1 sivA] {{PubMed|22383849}}
  
 
* '''[[Sigma factor]]:'''  
 
* '''[[Sigma factor]]:'''  
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[AbrB]]: transcription repression {{PubMed|20817675}}
  
−
* '''Additional information:'''  
+
* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
 +
<pubmed>18957862, 12823818 22571672 23335417 20817675</pubmed>
  
−
# Voigt et al. (2009) Cell physiology and protein secretion of ''Bacillus licheniformis'' compared to ''Bacillus subtilis''. ''J Mol Microbiol Biotechnol.'' '''16:''' 53-68 [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
+
[[Category:Protein-coding genes]]
−
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 

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)

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