Abstract
The data presented in this article are related to the publication entitled “Malonylome analysis of rhizobacterium Bacillus amyloliquefaciens FZB42 reveals involvement of lysine malonylation in polyketide synthesis and plant–bacteria interactions”(doi:10.1016/j.jprot.2016.11.022) (B. Fan, Y. Li, L. Li et al.) [1]. This article presented the raw information of all malonyllysine sites identified by LC-MS/MS in the Bacillus amyloliquefaciens FZB42. Further, the functional features and conservation of the malonylated peptide/proteins were analyzed and made publicly available to enable critical or extended analyses.
Highlights
Data ArticleMalonylome of the plant growth promoting rhizobacterium with potent biocontrol activity, Bacillus amyloliquefaciens FZB42
Proteins were extracted from the culture of Bacillus amyloliquefaciens FZB42 and digested by trypsin
The digested proteins were fractionated by HPLC before the peptides containing malonylation were enriched by anti-malonyllysine antibody beads
Summary
Malonylome of the plant growth promoting rhizobacterium with potent biocontrol activity, Bacillus amyloliquefaciens FZB42. The data presented in this article are related to the publication entitled “Malonylome analysis of rhizobacterium Bacillus amyloliquefaciens FZB42 reveals involvement of lysine malonylation in polyketide synthesis and plant–bacteria interactions”(http://dx. This article presented the raw information of all malonyllysine sites identified by LC-MS/MS in the Bacillus amyloliquefaciens FZB42. The functional features and conservation of the malonylated peptide/proteins were analyzed and made publicly available to enable critical or extended analyses.
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