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In past work, we have shown that the staphylococcal area necessary protein Bap, a member associated with the Biofilm-Associated Proteins (BAP) family members, is prepared in addition to fragments containing the N-terminal region become aggregation-prone and self-assemble into amyloid-like frameworks. Here, we report that Esp, a Bap-orthologous protein created by Enterococcus faecalis, shows an identical amyloidogenic behavior. We indicate that at acidic pH the N-terminal area

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