Fig. 2

Multiple sequence alignment. a Multiple sequence alignment between LipM and other closely family I.3 Lipases: AHB29478, LipM from Pseudomonas moraviensis M9; 2z8x, PML from Pseudomonas sp. MIS38; WP_010460388, LipT from Pseudomonas mandelii JR-1; AAP76488 and AAP76489, LipA and LipB from uncultured bacterium; ABY86751, lip35 from Pseudomonas sp. lip35; AFP20145, Lip I.3 from Pseudomonas sp. CR-611. Empty triangles (△) represent putative catalytic residues at the corresponding positions of Ser₁₅₃, Asp₂₀₂ and His₂₆₀. Sequence alignment was performed with Cluster 1.83 and visualized using ESpript 2.2. The alpha helix, beta sheet, random coil and beta turn are identical to α, β, η and T, respectively. 1: T5 primer; 2: T3 primer; 3: conserved catalytic motif; 4-5: the repetitive nine-residue motif GGXGXDXUX; 6: 18-residue amphipathic α-helix; 7: hydrophobic five-residue conserved motif; 8: four hydrophobic residues