DltB

• Description: D-alanine transfer from Dcp to undecaprenol-phosphate, alanylation of teichoic acid provides some resistance against positively charged antimicrobial peptides
  
  

Gene name	dltB
Synonyms	ipa-4r
Essential	no
Product	D-alanine transfer from Dcp to undecaprenol-phosphate
Function	biosynthesis of teichoic acid acid (D-alanyl transfer from Dcp to undecaprenol-phosphate)
Gene expression levels in SubtiExpress: dltB acid (D-alanyl transfer from Dcp to undecaprenol-phosphate)
MW, pI	46 kDa, 9.944
Gene length, protein length	1185 bp, 395 aa
Immediate neighbours	dltA, dltC
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, transporters/ other, biosynthesis of cell wall components, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins

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: BSU38510

Phenotypes of a mutant

• more sensitive to nisin PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: membrane-bound acyltransferase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • membrane associated PubMed

Database entries

• Structure:

• UniProt: P39580

• KEGG entry: [3]

• E.C. number:

Expression and regulation

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

• Expression browser: dltB 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:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I 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)

K Stephenson, C L Jensen, S T Jørgensen, C R Harwood
Simultaneous inactivation of the wprA and dltB genes of Bacillus subtilis reduces the yield of alpha-amylase.
Lett Appl Microbiol: 2002, 34(6);394-7
[PubMed:12028417] [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)