Difference between revisions of "CwlT"

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* '''Locus tag:''' BSU04970
 
* '''Locus tag:''' BSU04970
 
[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yddH_544022_545011_1 Expression]
 
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 19:48, 27 January 2012

  • Description: cell wall hydrolase, C-terminal domain hydrolyzes bond between D-Glu and m-DAP

Gene name cwlT
Synonyms yddH
Essential
Product cell wall hydrolase
Function cell wall metabolism
MW, pI 36 kDa, 8.632
Gene length, protein length 987 bp, 329 aa
Immediate neighbours yddG, yddI
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YddH 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

The gene

Basic information

  • Locus tag: BSU04970

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: nlpC/p60 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • induced by mitomycin C 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

Tatsuya Fukushima, Toshihiko Kitajima, Hiroyuki Yamaguchi, Qin Ouyang, Kazumi Furuhata, Hiroki Yamamoto, Toshio Shida, Junichi Sekiguchi
Identification and characterization of novel cell wall hydrolase CwlT: a two-domain autolysin exhibiting n-acetylmuramidase and DL-endopeptidase activities.
J Biol Chem: 2008, 283(17);11117-25
[PubMed:18305117] [WorldCat.org] [DOI] (P p)