Dataset for: Bacteriocin ASM1 is an O/S-diglycosylated, plasmid-encoded homologue of glycocin F

Lactobacillus plantarum A-1 secretes bacteriocin ASM1, with a calculated monoisotopic mass of 4642.8454 Da (based on the 43 amino acid sequence) and a measured mass of 5044.9727 Da. Here we show that ASM1 is a glycocin (glycosylated bacteriocin) with O- and S-linked N-acetylglucosamine moieties identical to glycocin F (GccF), and that the roles of specific structural features of ASM1 are very similar to GccF. Analysis of Lb. plantarum A-1 genomic DNA sequences showed that asm gene organisation (asmH←→asmABCDE→F) is identical to the gcc gene cluster, and that the asm genes reside on the novobiocin-curable 11,905-bp plasmid pA1_ASM1. Amino acid sequence identity averages ~69% across all Asm and Gcc proteins, and is highest for the identical ASM1/GccF peptide scaffold residues 1-30.

植物乳杆菌A-1可分泌细菌素ASM1，经计算其单同位素质量为4642.8454 Da（基于43个氨基酸的序列），实测质量为5044.9727 Da。本研究表明，ASM1是一种糖基化细菌素（glycocin），其O-连接与S-连接的N-乙酰葡糖胺（N-acetylglucosamine）修饰基团与糖基化细菌素F（GccF）完全一致，且ASM1的特定结构特征所发挥的功能与GccF高度相似。对植物乳杆菌A-1的基因组DNA序列分析显示，asm基因的排布（asmH←→asmABCDE→F）与gcc基因簇（gene cluster）完全一致，且asm基因位于新生霉素可消除的11905 bp质粒pA1_ASM1上。所有Asm与Gcc蛋白的平均氨基酸序列一致性约为69%，其中ASM1/GccF的肽骨架（peptide scaffold）1~30位氨基酸残基完全相同。