Genome sequence of the epiphytic bacteria Bacillus altitudinis strain 19_A, isolated from the marine macroalga Ulva lactuca

Abstract

Microorganisms living on marine macroalgal surfaces require enzyme repertoires to metabolize macroalgal-synthesized compounds. These enzymes are biological catalysts which have specific functional properties for biotechnological applications. Here, we raise awareness on the set of enzyme categories produced by the Bacillus altidudinis strain 19_A, isolated from the marine macroalga Ulva lactuca, as revealed by the analysis of its complete genome sequence. The genome of B. altitudinis strain 19_A is ∼3.7 Mb long, has a G + C content of 41.2 %, and contains a total of 3,967 protein-coding genes. Our predictive analysis revealed that these genes encode proteases, lipases, esterases, and enzymes involved in the synthesis, degradation, and modification of carbohydrates. This enzyme repertoire may have promising biotechnological and industrial applications.

Keywords: Bacillus altitudinis; Enzymes; Genome; Macroalgae.

Fig. 1

Map of the Bacillus altitudinis strain 19_A genome. Ticked inner and outer most circles serve as size references. In-between and going inwards, circles 1 and 2 display the CDCs on the forward strand (orange) and reverse strand (red), respectively. Circle 3 displays the GC percentage plot. Circle 4 displays the GC skew (purple above average, green below average). Circle 5 displays the COG categories. The genome map was made using GView Server [10].

Fig. 2

Phylogenetic tree derived from 16S rRNA gene sequence data. Analyses were conducted in MEGA7 [11] and the distances were computed using the Maximum Likelihood method. A bootstrap test was performed on the clusters in 1000 replicates. Bootstrap values are displayed as percentages on their relative branches. The 16S rRNA sequence of Lactococcus lactis was employed as the outgroup.

Fig. 3

Multiple amino acid sequence alignment of PL1_BA and other pectate lyases. The pectate lyases used were: BAA76884.1 from Bacillus sp. strain KSM-P7, ACD11362.1 from B. pumilus DKS1, BAA76885.1 from Bacillus sp. KSM-P103, ACY38198.1 from Bacillus sp. N16-5, and SV11.BT from Bacillus tequilensis SV11. Identical residues are within frames in red. marks the essential catalytic bases. marks the position of the three conserved aspartate residues for Ca²⁺ binding. The slender arrow shows the cleavage site of the signal peptide of PL1_BA.