Phyre 2 structures from Zinc binding proteome of a phytopathogen <i>Xanthomonas translucens</i> pv. <i>undulosa</i>.

<i>Xanthomonas translucens</i> pv. <i>undulosa</i> (<i>Xtu</i>) is a proteobacteria which causes bacterial leaf streak (BLS) or bacterial chaff disease in wheat and barley. The constant competition for zinc (Zn) metal nutrients contributes significantly in plant–pathogen interactions. In this study, we have employed a systematic <i>in silico</i> approach to study the Zn-binding proteins of <i>Xtu.</i> From the whole proteome of <i>Xtu</i>, we have identified ̴approximately 7.9% of proteins having Zn-binding sequence and structural motifs<i>.</i> Further, 115 proteins were found homologous to plant–pathogen interaction database. Among these 115 proteins, 11 were predicted as putative secretory proteins. The functional diversity in Zn-binding proteins was revealed by functional domain, gene ontology and subcellular localization analysis. The roles of Zn-binding proteins were found to be varied in the range from metabolism, proteolysis, protein biosynthesis, transport, cell signalling, protein folding, transcription regulation, DNA repair, response to oxidative stress, RNA processing, antimicrobial resistance, DNA replication and DNA integration. This study provides preliminary information on putative Zn-binding proteins of <i>Xtu</i> which may further help in designing new metal-based antimicrobial agents for controlling BLS and bacterial chaff infections on staple crops.