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Here, we describe functional characterization of an early gene ( gp46 ) product of a virulent  Lactococcus lactis  sk1 - like phage, vB_Llc_bIBBF13 (abbr. F13). The GP46  F 13  protein carries a catalytically active RecA-like domain belonging to the P-loop NTPase superfamily. It also retains features characteristic for ATPases forming oligomers. In order to elucidate its detailed molecular function, we cloned and overexpressed the  gp46  gene in  Escherichia coli . Purified GP46  F 13  protein binds to DNA and exhibits DNA unwinding activity on branched substrates in the presence of adenosine triphosphate (ATP). Size exclusion chromatography with multi-angle light scattering (SEC-MALS) experiments demonstrate that GP46  F 13  forms oligomers, and further pull-down assays show that GP46  F 13  interacts with host proteins involved in replication (i.e., DnaK, DnaJ, topoisomerase I, and single-strand binding protein). Taking together the localization of the gene and the obtained results, GP46  F 13  is the first protein encoded in the early-expressed gene region with helicase activity that has been identified among lytic  L. lactis  phages up to date.

An Adenosine Triphosphate- Dependent 5′-3′ DNA Helicase From sk1-Like Lactococcus lactis F13 Phage