Difference between revisions of "DltC"

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==Original publications==
 
==Original publications==
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<pubmed>14762009,15955059,26193422,7797557, 23980836 21856855,21926231</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:10, 21 July 2015

  • Description: D-alanine carrier protein, alanylation of teichoic acid provides some resistance against positively charged antimicrobial peptides

Gene name dltC
Synonyms ipa-3r
Essential no
Product D-alanine carrier protein
Function biosynthesis of teichoic acid
Gene expression levels in SubtiExpress: dltC
Metabolic function and regulation of this protein in SubtiPathways:
DltC
MW, pI 8 kDa, 3.621
Gene length, protein length 234 bp, 78 aa
Immediate neighbours dltB, dltD
Sequences Protein DNA DNA_with_flanks
Genetic context
DltC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DltC expression.png















Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, cell envelope stress proteins (controlled by SigM, V, W, X, Y)

This gene is a member of the following regulons

SigD regulon, SigM regulon, SigX regulon, Spo0A regulon, stringent response, YvrHb regulon

The gene

Basic information

  • Locus tag: BSU38520

Phenotypes of a mutant

  • more sensitive to nisin PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate) (according to Swiss-Prot)
  • 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: [3]

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
    • expression is reduced in a SigV mutant PubMed
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1394 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 3427 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Matthew G Percy, Angelika Gründling
Lipoteichoic acid synthesis and function in gram-positive bacteria.
Annu Rev Microbiol: 2014, 68;81-100
[PubMed:24819367] [WorldCat.org] [DOI] (I p)


Original publications

Stephan Zimmermann, Sabrina Pfennig, Piotr Neumann, Huma Yonus, Ulrich Weininger, Michael Kovermann, Jochen Balbach, Milton T Stubbs
High-resolution structures of the D-alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo- and holo-forms.
FEBS Lett: 2015, 589(18);2283-9
[PubMed:26193422] [WorldCat.org] [DOI] (I p)

Anthony W Kingston, Xiaojie Liao, John D Helmann
Contributions of the σ(W) , σ(M) and σ(X) regulons to the lantibiotic resistome of Bacillus subtilis.
Mol Microbiol: 2013, 90(3);502-18
[PubMed:23980836] [WorldCat.org] [DOI] (I p)

Veronica Guariglia-Oropeza, John D Helmann
Bacillus subtilis σ(V) confers lysozyme resistance by activation of two cell wall modification pathways, peptidoglycan O-acetylation and D-alanylation of teichoic acids.
J Bacteriol: 2011, 193(22);6223-32
[PubMed:21926231] [WorldCat.org] [DOI] (I p)

Theresa D Ho, Jessica L Hastie, Peter J Intile, Craig D Ellermeier
The Bacillus subtilis extracytoplasmic function σ factor σ(V) is induced by lysozyme and provides resistance to lysozyme.
J Bacteriol: 2011, 193(22);6215-22
[PubMed:21856855] [WorldCat.org] [DOI] (I p)

Juergen J May, Robert Finking, Frank Wiegeshoff, Thomas T Weber, Nina Bandur, Ulrich Koert, Mohamed A Marahiel
Inhibition of the D-alanine:D-alanyl carrier protein ligase from Bacillus subtilis increases the bacterium's susceptibility to antibiotics that target the cell wall.
FEBS J: 2005, 272(12);2993-3003
[PubMed:15955059] [WorldCat.org] [DOI] (P p)

Min Cao, John D Helmann
The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.
J Bacteriol: 2004, 186(4);1136-46
[PubMed:14762009] [WorldCat.org] [DOI] (P p)

M Perego, P Glaser, A Minutello, M A Strauch, K Leopold, W Fischer
Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation.
J Biol Chem: 1995, 270(26);15598-606
[PubMed:7797557] [WorldCat.org] [DOI] (P p)