Difference between revisions of "CwlO"
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− | * '''Description:''' endopeptidase-type autolysin <br/><br/> | + | * '''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 | + | |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) | + | * '''[[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 === | ||
Line 97: | Line 101: | ||
* '''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 This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
cell wall degradation/ turnover
This gene is a member of the following regulons
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:
Database entries
- Structure:
- UniProt: P40767
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor: SigA (according to PubMed)
- 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)