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] | ||
|- | |- | ||
|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:''' | ||
− | * ''' | + | * '''[[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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell wall synthesis, 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
- 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:
- 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
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)