LdcB

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell wall synthesis

The gene

Basic information

• Locus tag: BSU19620

Database entries

• BsubCyc: BSU19620

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization:
  • extracellular (signal peptide) PubMed

Database entries

• BsubCyc: BSU19620

• Structure:

• UniProt: O34866

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: deoD-ldcB PubMed

• Expression browser: ldcB PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)