DltA

• 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
Metabolic function and regulation of this protein in SubtiPathways: DltA
MW, pI	55 kDa, 4.929
Gene length, protein length	1509 bp, 503 aa
Immediate neighbours	ywzH, dltB
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, 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
• more sensitive to nisin PubMed

Database entries

• BsubCyc: BSU38500

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU38500

• Structure: 3E7X

• UniProt: P39581

• KEGG entry: [3]

• E.C. number: 6.1.1.13

Expression and regulation

• Operon: dltA-dltB-dltC-dltD-dltE PubMed

• Expression browser: dltA PubMed

• Sigma factor: SigD PubMed, SigM PubMed, SigX PubMed

• 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

• Regulatory mechanism:
  • activated by YvrHb PubMed
  • Spo0A: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1023 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2317 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1049 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 831 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 757 PubMed

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

References

Original publications

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)

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)