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Fig. 3 | Annals of Microbiology

Fig. 3

From: In vivo functional expression of an extracellular Ca2+-independent Bacillus pumilus lipase in Bacillus subtilis WB800N

Fig. 3

The amino acid residues analysis. a Rooted phylogenetic tree of LipBP. The consensus amino acid residues of LipBP and some homologous lipase were aligned with FASTA and GENEDOC. The sequences used in this alignment were obtained from GenBank as follows. 1: Lipase from Bacillus sp. HH-01 (GI:300116986), 2: Lipase from B. amyloliquefaciens subsp. plantarum YAU B9601-Y2 (GI:380496984), 3: Lipase from B. amyloliquefaciens XH7 (GI:341825903), 4: Lipase from B. atrophaeus 1942 (GI:310867486), 5: Lipase from B. licheniformis 9945A (GI:170878073), 6: Lipase from B. licheniformis ATCC14580 (GI:51507668), 7: Lipase from B. pumilus F3 (GI:118340982), 8: Lipase from B. pumilus XJU-13 (GI:130750924), 9: Lipase from B. pumilus Nws-bp1 used in this study (GI:544191646), 10: Lipase from B. megaterium QM B1551 (GI:294346812), 11: Lipase from B. megaterium DSM319 (GI:294799901). b, c Conserved sequence alignment of LipBP. The structures are denoted as follows: black triangle, the catalytic site (Ser111, Asp167, His190). The reserved amino acid motif AHSXG is boxed. The consensus amino acid residues for the signal peptide are underlined

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