Difference between revisions of "CwlO"

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(Extended information on the protein)
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* '''Description:''' endopeptidase-type autolysin <br/><br/>
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* '''Description:''' D,L-endopeptidase-type autolysin <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || endopeptidase-type autolysin  
 
|style="background:#ABCDEF;" align="center"| '''Product''' || endopeptidase-type autolysin  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || cell wall synthesis
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|style="background:#ABCDEF;" align="center"|'''Function''' || cell wall synthesis, cell proliferation
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 50 kDa, 5.326   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 50 kDa, 5.326   
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
a ''[[cwlO]] [[lytE]]'' mutant is not viable {{PubMed|17581128}}
+
a ''[[cwlO]] [[lytE]]'' mutant is not viable {{PubMed|17581128,22139507}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Protein family:''' peptidase C40 family (according to Swiss-Prot)
 
* '''Protein family:''' peptidase C40 family (according to Swiss-Prot)
  
* '''Paralogous protein(s):'''
+
* '''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 ===
 
=== Extended information on the protein ===
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* '''Domains:'''  
 
* '''Domains:'''  
 +
** C-terminal D,L-endopeptidase domain {{PubMed|22139507}}
  
 
* '''Modification:'''
 
* '''Modification:'''
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
  
* '''[[Localization]]:''' secreted (according to Swiss-Prot)extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
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* '''[[Localization]]:'''  
 +
** secreted (according to Swiss-Prot)
 +
** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
 +
** localizes to the lateral sidewall of the cell (via the N-terminal domain) {{PubMed|22139507}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Operon:'''  
 
* '''Operon:'''  
  
* '''[[Sigma factor]]:'''  
+
* '''[[Sigma factor]]:''' [[SigA]] (according to {{PubMed|22139507}})
  
 
* '''Regulation:''' activated by [[WalR]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17581128 PubMed]
 
* '''Regulation:''' activated by [[WalR]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17581128 PubMed]
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=References=
 
=References=
 
'''Additional publications:''' {{PubMed|21478646}}  
 
'''Additional publications:''' {{PubMed|21478646}}  
<pubmed>16233686,17581128, 20525796,18957862, 20059685 </pubmed>
+
<pubmed>16233686,17581128, 20525796,18957862, 20059685 ,22139507</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:04, 8 December 2011

  • Description: D,L-endopeptidase-type autolysin

Gene name cwlO
Synonyms yzkA, yvcE
Essential no
Product endopeptidase-type autolysin
Function cell wall synthesis, cell proliferation
MW, pI 50 kDa, 5.326
Gene length, protein length 1419 bp, 473 aa
Immediate neighbours trxB, yvcD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvcE context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell wall degradation/ turnover

This gene is a member of the following regulons

WalR regulon

The gene

Basic information

  • Locus tag: BSU34800

Phenotypes of a mutant

a cwlO lytE mutant is not viable PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: peptidase C40 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:
  • Domains:
    • C-terminal D,L-endopeptidase domain PubMed
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • secreted (according to Swiss-Prot)
    • extracellular (signal peptide) PubMed
    • localizes to the lateral sidewall of the cell (via the N-terminal domain) PubMed

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • Regulatory mechanism:
  • Additional information:
    • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

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)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [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)

Paola Bisicchia, David Noone, Efthimia Lioliou, Alistair Howell, Sarah Quigley, Thomas Jensen, Hanne Jarmer, Kevin M Devine
The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis.
Mol Microbiol: 2007, 65(1);180-200
[PubMed:17581128] [WorldCat.org] [DOI] (P p)

Hiroyuki Yamaguchi, Kazumi Furuhata, Tatsuya Fukushima, Hiroki Yamamoto, Junichi Sekiguchi
Characterization of a new Bacillus subtilis peptidoglycan hydrolase gene, yvcE (named cwlO), and the enzymatic properties of its encoded protein.
J Biosci Bioeng: 2004, 98(3);174-81
[PubMed:16233686] [WorldCat.org] [DOI] (P p)