Identification and
systematic analysis of candidates for protein
propionylation are crucial steps for understanding its molecular mechanisms
and biological functions. Although several proteome-scale methods
have been performed to delineate potential propionylated proteins,
the majority of lysine-propionylated substrates and their role in
pathological physiology still remain largely unknown. By gathering
various databases and literatures, experimental prokaryotic propionylation
data were collated to be trained in a support vector machine with
various features via a three-step feature selection method. A novel
online tool for seeking potential lysine-propionylated sites (PropSeek)
(http://bioinfo.ncu.edu.cn/PropSeek.aspx) was built. Independent test results of leave-one-out and n-fold cross-validation were similar to each other, showing
that PropSeek is a stable and robust predictor with satisfying performance.
Meanwhile, analyses of Gene Ontology, Kyoto Encyclopedia of Genes
and Genomes pathways, and protein–protein interactions implied
a potential role of prokaryotic propionylation in protein synthesis
and metabolism.