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This is the very C-terminal, chaperone, domain of thebacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, Pfam:PF12219. The endosialidase protein forms homotrimeric molecules in bacteriophages [1]. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and presumably bind to DNA.
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