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Figure S1: Kinetic stability at 60°C for two wild type and three consensus SP enzymes.

Figure S2: MSA of the top correlated positions in the lactic acid bacteria-like SP subset. Positions with a correlation coefficient >0.8 are shown with their 3D number and their total number of correlations of which the co-evolution network is shown in Figure S3. The alignment is divided in the LAB-like SP sequences (top) and the Bifidobacteria-like SP sequences (bottom). Amino acids are colored by residue type.

Figure S3A: Co-evolution network for 3DM positions of the multiple sequence alignment of lactic acid bacteria-like SPs. B: The correlating positions are visualized as red balls in the crystal structure of BaSP (2GDU chain A).

Figure S4: MSA of the top correlated positions in the Bifidobacteria-like SP subset. Positions with a correlation coefficient >0.8 are shown with their 3D number and their total number of correlations of which the co-evolution network is shown in Figure S5. The alignment is divided in the LAB-like SP sequences (top) and the Bifidobacteria-like SP sequences (bottom). Amino acids are colored by residue type.

Figure S5A: Co-evolution network for 3DM positions of the multiple sequence alignment of Bifidobacteria-like SPs. B: The correlating positions are visualized as green balls in the crystal structure of BaSP (2GDU chain A).

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