Difference between revisions of "CwlT"

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* '''Description:''' cell wall hydrolase, required for conjugation of ICE''Bs1'', C-terminal domain hydrolyzes bond between D-Glu and m-DAP <br/><br/>
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* '''Description:''' cell wall hydrolase, required for conjugation of ICE''Bs1'', part of the type IV secretion system for DNA transfer , C-terminal domain hydrolyzes bond between D-Glu and m-DAP <br/><br/>
  
 
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|style="background:#ABCDEF;" align="center"| '''Product''' || cell wall hydrolase  
 
|style="background:#ABCDEF;" align="center"| '''Product''' || cell wall hydrolase  
 
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|style="background:#ABCDEF;" align="center"|'''Function''' || conjugation of ICE''Bs1''
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|style="background:#ABCDEF;" align="center"|'''Function''' || conjugative transfer of ICEBs1
 
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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=BSU04970 cwlT]
 
|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=BSU04970 cwlT]

Revision as of 16:04, 28 May 2015

  • Description: cell wall hydrolase, required for conjugation of ICEBs1, part of the type IV secretion system for DNA transfer , C-terminal domain hydrolyzes bond between D-Glu and m-DAP

Gene name cwlT
Synonyms yddH
Essential
Product cell wall hydrolase
Function conjugative transfer of ICEBs1
Gene expression levels in SubtiExpress: cwlT
MW, pI 36 kDa, 8.632
Gene length, protein length 987 bp, 329 aa
Immediate neighbours yddG, yddI
Sequences Protein DNA DNA_with_flanks
Genetic context
YddH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CwlT expression.png















Categories containing this gene/protein

mobile genetic elements, 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:
    • hydrolysis of peptidoglycan (linkage between N-acetylmuramic acid and N-acetylglucosamine and bond between D-γ-glutamate and meso-diaminopimelic acid) PubMed
  • Protein family: nlpC/p60 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • N-terminal domain is an N-acetylmuramidase that cleaves the linkage between N-acetylmuramic acid and N-acetylglucosamine PubMed
    • C-terminal endopeptidase domain cleaves the bond between D-γ-glutamate and meso-diaminopimelic acid PubMed
  • Modification:
  • Effectors of protein activity:
  • Localization:
    • secreted (with signal peptide) PubMed
    • may be a lipoprotein, but the lipid anchor is not required for function PubMed

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

Tyler DeWitt, Alan D Grossman
The bifunctional cell wall hydrolase CwlT is needed for conjugation of the integrative and conjugative element ICEBs1 in Bacillus subtilis and B. anthracis.
J Bacteriol: 2014, 196(8);1588-96
[PubMed:24532767] [WorldCat.org] [DOI] (I p)

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)