Campylobacter jejuni is the leading cause of bacterial gastroenteritis in the developed world. Infection occurs predominantly through the consumption of undercooked/poorly prepared commercial chicken products. Importantly, C. jejuni exists mainly as a commensal organism within the intestines of chickens, but is pathogenic in humans. While the exact mechanism of this difference in pathogenicity is unknown, factors such as motility and nutrient uptake are thought to be significant in the host-pathogen nexus. C. jejuni is generally considered assaccharolytic and primarily utilizes amino and organic acids as carbon sources, with only some strains able to utilize fucose. We conducted label-based LC-MS/MS proteome analysis of C. jejuni NCTC11168O to identify proteins associated with growth in deoxycholate, which mimics gut bile salts encountered during human infection. We quantified 1561 proteins (93% of the predicted C. jejuni proteome). The most significantly induced protein (mean 4.6-fold induction) was the product of the cj0025 gene, which has been previously annotated as a ‘putative C4-dicarboxylate transport protein’. To determine the function of Cj0025, metabolomic profiles of media inoculated with C. jejuni wild-type or a Δcj0025 deletion strain were compared, with focus on the uptake of amino acids and Krebs cycle intermediates. Our results showed that the both strains exhibited a preference for six amino acids – asparagine, cysteine, proline, serine, aspartate and glutamate, all of which, bar cysteine, were reduced to less than 15% of their initial concentration in rich media after 48 hours of inoculation. Both strains also showed the capacity to uptake most Krebs cycle intermediates. Therefore, the mutant was not defective for the uptake of any known C. jejuni amino acid or Krebs cycle intermediate carbon source under standard microaerobic conditions. This suggests Cj0025 may have a role in micro-nutrient transport and/or be responsible for transport of a nutrient with more than one active transporter.