Difference between revisions of "CwlS"

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* '''Description:''' D,L-endopeptidase, peptidoglycan hydrolase <br/><br/>
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* '''Description:''' D,L-endopeptidase, peptidoglycan hydrolase for cell separation<br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || D,L-endopeptidase, peptidoglycan hydrolase  
 
|style="background:#ABCDEF;" align="center"| '''Product''' || D,L-endopeptidase, peptidoglycan hydrolase  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || cell wall metabolism
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|style="background:#ABCDEF;" align="center"|'''Function''' || cell separation
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|-
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|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=BSU19410 cwlS]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 44 kDa, 10.438   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 44 kDa, 10.438   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yojM]]'', ''[[yojK]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yojM]]'', ''[[yojK]]''
 
|-
 
|-
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13833&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU19410 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU19410 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU19410 DNA_with_flanks]
 
|-
 
|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yojL_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yojL_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>
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|-
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cwlS_2115425_2116669_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:cwlS_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU19410]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
 
<br/><br/>
 
<br/><br/>
  
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=== Database entries ===
 
=== Database entries ===
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* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU19410&redirect=T BSU19410]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
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=== Additional information===
 
=== Additional information===
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−
 
  
  
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
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* '''Domains:'''  
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* '''[[Domains]]:'''  
 +
** contains four N-acetylglucosamine-polymer-binding [[LysM domain]]s {{PubMed|24355088,18430080}}
 
** C-terminal D,L-endopeptidase domain {{PubMed|22139507}}
 
** C-terminal D,L-endopeptidase domain {{PubMed|22139507}}
  
 
* '''Modification:'''
 
* '''Modification:'''
  
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* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU19410&redirect=T BSU19410]
  
 
* '''Structure:'''
 
* '''Structure:'''
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cwlS_2115425_2116669_-1 cwlS] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cwlS_2115425_2116669_-1 cwlS] {{PubMed|22383849}}
  
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* '''Sigma factor:''' [[SigD]], [[SigH]], according to {{PubMed|22139507}}
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* '''[[Sigma factor]]:''' [[SigD]], [[SigH]], according to {{PubMed|22139507}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
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'''Additional publications:''' {{PubMed|20817675}}
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== Reviews==
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<pubmed>16855244,12850135, 22139507 </pubmed>
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<pubmed>18430080</pubmed>
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== Original publications ==
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<pubmed>16855244,12850135, 22139507 20817675 24355088</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Latest revision as of 13:55, 2 April 2014

  • Description: D,L-endopeptidase, peptidoglycan hydrolase for cell separation

Gene name cwlS
Synonyms yojL
Essential no
Product D,L-endopeptidase, peptidoglycan hydrolase
Function cell separation
Gene expression levels in SubtiExpress: cwlS
MW, pI 44 kDa, 10.438
Gene length, protein length 1242 bp, 414 aa
Immediate neighbours yojM, yojK
Sequences Protein DNA DNA_with_flanks
Genetic context
YojL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CwlS expression.png















Categories containing this gene/protein

cell wall degradation/ turnover, membrane proteins

This gene is a member of the following regulons

Abh regulon, AbrB regulon, CcpA regulon, SigD regulon, SigH regulon,

The gene

Basic information

  • Locus tag: BSU19410

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm (according to Swiss-Prot)
  • Protein family: Cu-Zn superoxide dismutase family (according to Swiss-Prot)
  • Paralogous protein(s): the C-terminal D,L-endopeptidase domains of LytE, LytF, CwlS, and CwlO exhibit strong sequence similarity

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
  • Localization:
    • cell membrane (according to Swiss-Prot)
    • localizes to cell septa and poles PubMed

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
    • CcpA: transcription repression
    • Abh and AbrB: synergistic transcription repression PubMed
  • 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

Reviews

Original publications

Jaslyn E M M Wong, Husam M A B Alsarraf, Jørn Døvling Kaspersen, Jan Skov Pedersen, Jens Stougaard, Søren Thirup, Mickaël Blaise
Cooperative binding of LysM domains determines the carbohydrate affinity of a bacterial endopeptidase protein.
FEBS J: 2014, 281(4);1196-208
[PubMed:24355088] [WorldCat.org] [DOI] (I p)

Masayuki Hashimoto, Seika Ooiwa, Junichi Sekiguchi
Synthetic lethality of the lytE cwlO genotype in Bacillus subtilis is caused by lack of D,L-endopeptidase activity at the lateral cell wall.
J Bacteriol: 2012, 194(4);796-803
[PubMed:22139507] [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)

Tatsuya Fukushima, Anahita Afkham, Shin-Ichirou Kurosawa, Taichi Tanabe, Hiroki Yamamoto, Junichi Sekiguchi
A new D,L-endopeptidase gene product, YojL (renamed CwlS), plays a role in cell separation with LytE and LytF in Bacillus subtilis.
J Bacteriol: 2006, 188(15);5541-50
[PubMed:16855244] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

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