Extended Data Figure 1 : Multiple amino acid sequence alignment of YidC proteins.

From: Structural basis of Sec-independent membrane protein insertion by YidC

Extended Data Figure 1

Sequence alignment of Bacillus halodurans YidC2 (BhYidC2), B. halodurans YidC1 (BhYidC1), Bacillus subtilis SpoIIIJ (BsSpoIIIJ), B. subtilis YidC2 (BsYidC2) and Escherichia coli YidC (EcYidC). The secondary structure of YidC27–266 is indicated above the sequences. The α-helices (as described in the main text) and β-strands (ES1 and ES2 in the E2 region) are indicated by cylinders and arrows, respectively. Strictly conserved residues among the five molecules are highlighted in red boxes, and highly conserved residues are indicated by red letters. The hydrophilic and bulky residues that were mutated and the pBpa positions introduced into B. halodurans YidC2 are indicated by grey, green and blue triangles, respectively. The spoIIIJ K248stop derivative has a stop codon introduced at position 248, as indicated, and thereby expresses a SpoIIIJ mutant that lacks the C-terminal 14 residues.