Glycopeptide antibiotics (GPAs) - e.g. vancomycin - are natural products that have been used for many years as a last resort and are an important group of agents to fight bacterial infections (e.g. MRSA) by inhibiting cell wall biosynthesis. Numerous GPA producers have been found in the genera Amycolatopsis or Streptomyces within the phylum of Actinobacteria.

GPAs are modified peptides consisting of proteinogenic and non-proteinogenic amino acids (n=7-10). However, glycosylation and modification of the peptide backbone leads to a large variety of different structures. All relevant proteins involved in building block supply, biosynthesis and peptide modification are encoded in a biosynthetic gene cluster (BGC). The biosynthesis is carried out by non-ribosomal peptide synthetases (NRPS). Interestingly, a transport-related protein is always co-encoded within the respective BGC. 

In this project, we address the question of whether these transporters, which are often ATP-binding cassette transporters, are specific for their cognate substrate. In addition, we are investigating possible interactions between the transporter and the biosynthetic machinery that may enhance production efficiency.