Structural component of the short non-contractile tail. The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane. Homotrimer. Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O-antigen. The interdigitation of the polypeptide chains at the C-termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein. Belongs to the P22likevirus tail fiber protein family.