KMP11 is an essential and highly conserved kinetoplastid protein. Using immunofluorescence, ultrastructure expansion microscopy and pulldown experiments, we show that KMP11 localizations in Trypanosoma brucei include the flagellum attachment zone, the paraflagellar rod, the flagellar connector, the microtubule quartet and the central alpha-helical domain of the tripartite attachment complex subunit p197. However, unlike previously reported, KMP11 does not localize to the basal body. Expansion microscopy and pulldown experiments furthermore showed that T. brucei KMP11 also binds to the central domain of T. cruzi p197. The central domains of p197 from the two species do not share a sequence homology but both have a high alpha-helical content. Thus, KMP11 may not bind to a specific peptide but to a common structural element of alpha-helices. KMP11 forms a rod-shaped homodimer which would be consistent with a crosslinking function. Thus, we speculate that KMP11 forms bundles between p197 molecules, and between other cytoskeletal proteins with a high alpha-helical content, offering a unifying model for its widespread localization.