The twin-arginine translocation (Tat) system is specialized in the transport of folded proteins across the cytoplasmic membrane. Although the mechanisms that govern the Tat transport and its scope are not well understood, this system and its cognate substrates are involved in important functions that facilitate the adaptation and survival of bacteria. Evidence also exists that connects the Tat system to virulent traits of clinically relevant pathogens. Of interest is Campylobacter jejuni, an important foodborne pathogen that is capable of surviving in different hosts and environmental niches. Recent studies have shown that the Tat system in this bacterium mediates key metabolic and stress resistance traits. Furthermore, the majority of the identified Tat substrates in C. jejuni are cofactor-containing redox proteins that contribute to the bacterium?s branched electron transport chain, a component essential for survival under differing conditions. These studies as well as the absence of Tat homologs in the sequenced genomes of animals suggest that the Tat system might pose an attractive target for therapeutics against C. jejuni.