Fig. 1: Prediction of the amyloidogenic potential of Esp.
From: The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers
a Structural similarity between Bap and Esp. The N-terminal domain of Esp (residues 49–743) and region B of Bap (residues 361–819) share 26% sequence identity. The C-repeats of Bap (amino acids 820–2147) and C-repeats of Esp (amino acids 1064–1648) share 23% sequence identity. b Comparison of the predicted aggregation propensities. Bars representing the aggregation propensities obtained by four bioinformatic algorithms TANGO (violet), Aggrescan (orange), WALTZ (black), and FoldAmyloid (Blue). Values have been normalized for each predictor. Asterisks denote the amino acid stretches predicted to be amyloidogenic by at least three of the algorithms used.
