Difference between revisions of "DltA"

From SubtiWiki
Jump to: navigation, search
Line 1: Line 1:
* '''Description:''' D-alanyl-D-alanine carrier protein ligase, alanylation of phosphatidylglycerol provides some resistance against positively charged antimicrobial peptides <br/><br/>
+
* '''Description:''' D-alanyl-D-alanine carrier protein ligase, alanylation of teichoic acid provides some resistance against positively charged antimicrobial peptides <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  

Revision as of 13:54, 31 October 2012

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

Gene name dltA
Synonyms ipa-5r, dae
Essential no
Product D-alanyl-D-alanine carrier protein ligase
Function biosynthesis of teichoic acid
Gene expression levels in SubtiExpress: dltA
MW, pI 55 kDa, 4.929
Gene length, protein length 1509 bp, 503 aa
Immediate neighbours menA, dltB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DltA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DltA 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: BSU38500

Phenotypes of a mutant

    • increased sensitivity to lysozyme 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: DltA subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • 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:

Biological materials

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

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

Your additional remarks

References

Additional publications: PubMed

Khan Tanjid Osman, Liqin Du, Yujiong He, Yu Luo
Crystal structure of Bacillus cereus D-alanyl carrier protein ligase (DltA) in complex with ATP.
J Mol Biol: 2009, 388(2);345-55
[PubMed:19324056] [WorldCat.org] [DOI] (I p)

Huma Yonus, Piotr Neumann, Stephan Zimmermann, Jürgen J May, Mohamed A Marahiel, Milton T Stubbs
Crystal structure of DltA. Implications for the reaction mechanism of non-ribosomal peptide synthetase adenylation domains.
J Biol Chem: 2008, 283(47);32484-91
[PubMed:18784082] [WorldCat.org] [DOI] (P p)

Masakuni Serizawa, Keisuke Kodama, Hiroki Yamamoto, Kazuo Kobayashi, Naotake Ogasawara, Junichi Sekiguchi
Functional analysis of the YvrGHb two-component system of Bacillus subtilis: identification of the regulated genes by DNA microarray and northern blot analyses.
Biosci Biotechnol Biochem: 2005, 69(11);2155-69
[PubMed:16306698] [WorldCat.org] [DOI] (P 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)