Difference between revisions of "LdcB"

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=References=
 
=References=
  
<pubmed>18957862, 24909784 22383849</pubmed>
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<pubmed>18957862, 24909784 22383849 21378199 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:09, 10 June 2014

  • Description: LD-carboxypeptidase, releases D-Ala from the cell wall

Gene name ldcB
Synonyms yodJ
Essential no
Product LD-carboxypeptidase
Function cell wall synthesis
Gene expression levels in SubtiExpress: ldcB
MW, pI 30 kDa, 5.84
Gene length, protein length 819 bp, 273 aa
Immediate neighbours yodI, deoD
Sequences Protein DNA DNA_with_flanks
Genetic context
YodJ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YodJ expression.png















Categories containing this gene/protein

cell wall synthesis

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU19620

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • trimming of cell wall peptides (tetrapeptides to tripeptides) wit concomitant release of D-ala PubMed
  • Protein family:
  • 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

  • Regulation:
  • 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

Christopher N Hoyland, Christine Aldridge, Robert M Cleverley, Marie-Clémence Duchêne, George Minasov, Olena Onopriyenko, Karzan Sidiq, Peter J Stogios, Wayne F Anderson, Richard A Daniel, Alexei Savchenko, Waldemar Vollmer, Richard J Lewis
Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition.
Structure: 2014, 22(7);949-60
[PubMed:24909784] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Skye M Barendt, Lok-To Sham, Malcolm E Winkler
Characterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39.
J Bacteriol: 2011, 193(9);2290-300
[PubMed:21378199] [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)