dltA

168

D-alanyl-D-alanine carrier protein ligase, alanylation of teichoic acid provides some resistance against positively charged antimicrobial peptides and against bacteriophage infection

Locus: BSU_38500

Molecular weight: 55.64 kDa

Isoelectric point: 4.93

Protein length: 503 aa

Gene length: 1512 bp

Function: biosynthesis of teichoic acid

Product: D-alanyl-D-alanine carrier protein ligase

Essential: no

E.C.: 6.1.1.13

Synonyms: dltA, ipa-5r, dae

Genomic Context

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List of homologs in different organisms, belongs to COG1020 (Galperin et al., 2021)

Gene

Coordinates: 3,952,275  3,953,786

Phenotypes of a mutant

• increased sensitivity to lysozyme PubMed
• more sensitive to nisin PubMed

The protein

Catalyzed reaction/ biological activity

• ATP + D-alanine + holo-DltC --> AMP + D-alanyl-DltC + diphosphate (according to UniProt) PubMed

Protein family

• ATP-dependent AMP-binding enzyme family (according to UniProt)

Structure

• 3E7X (PDB)
• P39581 (AlphaFold)

Localization

• cytoplasm (according to UniProt)

Expression and Regulation

Operons

• Genes: dltX-dltA-dltB-dltC-dltD-dltE

  Description: PubMed

  Regulation

  • expression is reduced in a SigV mutant PubMed
  • the mRNA is processed between dltX and dltA by RNase Y, this requires the RicA-RicF-RicT complex PubMed

  Regulatory mechanism

  • YvrHb: activation, PubMed, in yvrHb regulon
  • Spo0A: repression, PubMed, in spo0A regulon
  • stringent response: negative regulation, in stringent response

  Sigma factors

  • SigD: sigma factor, PubMed, in sigD regulon
  • SigM: sigma factor, PubMed, in sigM regulon
  • SigX: sigma factor, PubMed, in sigX regulon
  • SigV: sigma factor, PubMed, in sigV regulon

Biological materials

Mutant

• BKE38500 (dltA::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_TTTCATAGTTATTCTCTCTC,  downstream forward: _UP4_CGCATTGGCGAAGAGGTTCT
• BKK38500 (dltA::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_TTTCATAGTTATTCTCTCTC,  downstream forward: _UP4_CGCATTGGCGAAGAGGTTCT

Labs working on this gene/protein

• Mohamed Marahiel, Marburg University, Germany homepage

References

Reviews

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Original Publications

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