Difference between revisions of "CwlO"

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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=BSU34800 cwlO]
 
|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=BSU34800 cwlO]
 +
|-
 +
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=CwlO CwlO]
 
|-
 
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|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|17581128,22139507}}
 
* a ''[[cwlO]] [[lytE]]'' mutant is not viable {{PubMed|17581128,22139507}}
* shorter, fatter cells {{PubMed|23855774}}
+
* shorter, fatter cells, this can be rescued by addition of Mg(2+) {{PubMed|23869552,23855774}}
  
 
=== Database entries ===
 
=== Database entries ===
Line 77: Line 79:
 
* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
+
* '''[[Domains]]:'''  
 
** C-terminal D,L-endopeptidase domain {{PubMed|22139507}}
 
** C-terminal D,L-endopeptidase domain {{PubMed|22139507}}
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
** [[CwlO]] requires activation by [[FtsE]]-[[FtsX]] {{PubMed|23855774}}
+
** [[CwlO]] requires activation by [[FtsE]]-[[FtsX]] {{PubMed|23869552,23855774}}
 +
** activity requires functional [[Mbl]] {{PubMed|23869552}}
  
 
* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 +
** [[FtsX]]-[[CwlO]], at the membrane {{PubMed|23869552}}
  
 
* '''[[Localization]]:'''  
 
* '''[[Localization]]:'''  
 
** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
 
** extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
 
** localizes to the outer lateral sidewall of the cell (via the N-terminal domain) {{PubMed|22139507}}
 
** localizes to the outer lateral sidewall of the cell (via the N-terminal domain) {{PubMed|22139507}}
 +
** cell membrane in a FtsX-dependent manner {{PubMed|23869552}}
  
 
=== Database entries ===
 
=== Database entries ===
Line 111: Line 116:
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cwlO_3574363_3575784_-1 cwlO] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cwlO_3574363_3575784_-1 cwlO] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigA]] (according to {{PubMed|22139507}})
+
* '''[[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]
Line 142: Line 147:
 
<pubmed>23066944</pubmed>
 
<pubmed>23066944</pubmed>
 
== Original publications ==
 
== Original publications ==
<pubmed>21478646 16233686,17581128, 20525796,18957862, 20059685 ,22139507 23855774</pubmed>
+
<pubmed>21478646 16233686,17581128, 20525796,18957862, 20059685 ,22139507 23855774 23869552</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:34, 14 December 2013

  • Description: D,L-endopeptidase-type autolysin, primary autolytic pathway for cell elongation

Gene name cwlO
Synonyms yzkA, yvcE
Essential no
Product endopeptidase-type autolysin
Function cell wall synthesis, cell elongation
Gene expression levels in SubtiExpress: cwlO
Interactions involving this protein in SubtInteract: CwlO
MW, pI 50 kDa, 5.326
Gene length, protein length 1419 bp, 473 aa
Immediate neighbours trxB, yvcD
Sequences Protein DNA DNA_with_flanks
Genetic context
YvcE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CwlO expression.png















Categories containing this gene/protein

cell wall synthesis, 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
  • shorter, fatter cells, this can be rescued by addition of Mg(2+) 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:
  • Modification:
  • Localization:
    • extracellular (signal peptide) PubMed
    • localizes to the outer lateral sidewall of the cell (via the N-terminal domain) PubMed
    • cell membrane in a FtsX-dependent manner 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

Reviews

Original publications

Patricia Domínguez-Cuevas, Ida Porcelli, Richard A Daniel, Jeff Errington
Differentiated roles for MreB-actin isologues and autolytic enzymes in Bacillus subtilis morphogenesis.
Mol Microbiol: 2013, 89(6);1084-98
[PubMed:23869552] [WorldCat.org] [DOI] (I p)

Jeffrey Meisner, Paula Montero Llopis, Lok-To Sham, Ethan Garner, Thomas G Bernhardt, David Z Rudner
FtsEX is required for CwlO peptidoglycan hydrolase activity during cell wall elongation in Bacillus subtilis.
Mol Microbiol: 2013, 89(6);1069-83
[PubMed:23855774] [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)

Nobuo Mitsui, Hisashi Murasawa, Junichi Sekiguchi
Disruption of the cell wall lytic enzyme CwlO affects the amount and molecular size of poly-γ-glutamic acid produced by Bacillus subtilis (natto).
J Gen Appl Microbiol: 2011, 57(1);35-43
[PubMed:21478646] [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)