Acts as a primer for DNA elongation during viral genomic replication. Acts as the small terminase protein during packaging. Recruits the phage DNA polymerase to the bacterial nucleoid. Primer terminal protein (TP) is covalently linked to the 5'-ends of both strands of the genome through a phosphodiester bond between the beta-hydroxyl group of a serine residue and the 5'-phosphate of the terminal deoxyadenylate (dAMP). To start replication, the DNA polymerase forms a heterodimer with a free TP that recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP. Since the polymerase initiates the replication on the second thymine, the TP-dAMP initiation product slides backwards to recover the template information of the first nucleotide. Hydrolyzes host peptidoglycans during virus entry. Interacts with the viral polymerase; this interaction allows the initiation of TP-primed DNA replication at both viral DNA ends. Binds to ssDNA. Interacts with the replication protein p1. Part of a DNA-gp3-gp16 complex. Associates with the host bacterial nucleoid through its N-terminal region. Belongs to the phi29likevirus DNA terminal protein family.