Difference between revisions of "CwlS"
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=== Database entries === | === Database entries === | ||
| + | * '''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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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU19410&redirect=T BSU19410] | ||
* '''Structure:''' | * '''Structure:''' | ||
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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
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
- BsubCyc: BSU19410
- 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:
- Domains:
- contains four N-acetylglucosamine-polymer-binding LysM domains PubMed
- C-terminal D,L-endopeptidase domain PubMed
- Modification:
- Effectors of protein activity:
- Localization:
- cell membrane (according to Swiss-Prot)
- localizes to cell septa and poles PubMed
Database entries
- BsubCyc: BSU19410
- Structure:
- UniProt: O31852
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor: SigD, SigH, according to PubMed
- Regulatory mechanism:
- 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
Girbe Buist, Anton Steen, Jan Kok, Oscar P Kuipers
LysM, a widely distributed protein motif for binding to (peptido)glycans.
Mol Microbiol: 2008, 68(4);838-47
[PubMed:18430080]
[WorldCat.org]
[DOI]
(I p)
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)
