Conjugative type IV secretion systems (T4SSs) are multi-protein complexes in Gram-negative and Gram-positive (G+) bacteria, responsible for spreading antibiotic resistances and virulence factors among different species. Compared to Gram-negative bacteria, which establish close contacts for conjugative transfer via sex pili, G+ T4SSs are suggested to employ surface adhesins instead. One example is pCF10, an enterococcal conjugative sex-pheromone responsive plasmid with a narrow host range, thus disseminating genetic information only among closely related species. This MicroCommentary is dedicated to the crystal structure of the pCF10-encoded adhesion domain of PrgB presented by Schmitt et al. The authors show in their work that this adhesion domain is responsible for biofilm formation, tight binding and condensation of extracellular DNA (eDNA) and conjugative transfer of pCF10. A sophisticated two-step mechanism for highly efficient conjugative transfer is postulated, including the formation of PrgB-mediated long-range intercellular contacts by binding and establishment of shorter-range contacts via condensation of eDNA. PrgB binding to lipoteichoic acid on the recipient cell surface stabilizes junctions between the mating partners. The major findings by Schmitt et al. will be brought into a broader context and potential medical applications targeting eDNA as essential component in biofilm formation and conjugation will be discussed.