5-Oxoproline (OP), a natural amino acid derivative, is generated from the spontaneous cyclisation of glutamate and glutamine in vivo. Historically, OP has been viewed as a waste product which is toxic to bacteria. However, since the discovery of a bacterial 5-Oxoprolinase, which converts OP to glutamate, its possible role as a nutrient source has emerged, yet the basis of its assimilation is unknown. Here, we characterise an operon comprising three proteins of unknown function that are putatively involved in the transport and utilisation of OP by C. jejuni. DUF969/979 appear to form an OP transporter which may represent a new sub-class of the divalent anion-sodium symporter (DASS) family. DUF2891 encodes a cytoplasmic protein with no clear function, yet our experiments demonstrate all three genes are essential for the utilisation of OP. Through phylogenetic analyses, we identified these DUF proteins to be largely absent in Campylobacter species other than C. jejuni, where it is conversely ubiquitous. We also scanned over 6000 reference genomes, representing the available breadth of all bacterial species, revealing homologues of DUF969/979 in ~700 species (>10% of all bacteria), indicating the ability to import exogenous OP is common. Our findings provide new insights into the nutrient acquisition strategies of C. jejuni, expanding current understanding of its metabolic plasticity, as well as presenting a widespread bacterial capacity for OP transport and utilisation.