Campylobacter jejuni is the most prevalent cause of bacterial gastroenteritis worldwide. Although the molecular mechanisms of pathogenesis of this organism are poorly understood, motility and chemotaxis are known to play an important role. A rare C. jejuni chemotaxis receptor, initially named Tlp11, was first identified in a highly virulent clinical isolate C. jejuni 520. It was subsequently also found in a sequenced C. jejuni strain 84-25, isolated from a meningitis case. Tlp11 was found in clinical isolates that resulted in hospitalisation of infected individuals. Chemotaxis ligand and small molecule array screening determined galactose to be the ligand specific for this sensory receptor. Chemotaxis assays using wild type and isogenic inactivation, allelic addition and complemented mutant strains, confirmed the chemotactic response of C. jejuni to galactose was Tlp11 dependant. Motility and autoagglutination were significantly altered by Tlp11 expression with decrease in motility and increased autoagglutination in the tlp11 isogenic mutant, as opposed to wild type strain, similar to that seen for C. jejuni multiligand receptor CcmL. This novel C. jejuni receptor was consequently named CcrG, campylobacter chemoreceptor for galactose. C. jejuni 520 ccrG mutant was shown to have significantly reduced ability to adhere to Int-407 and Caco2 intestinal cells lines and significantly reduced ability to colonise chickens. Comparative genomic analysis of the CcrG sequence revealed that the sequence encoding this receptor is unique and likely to have arisen via fusion of periplasmic sensory domain of CcaA, the aspartate receptor, and signalling cytoplasmic domain of CcmL, the multiligand receptor. The findings in this study provide further insight into chemotaxis receptor protein-ligand interactions with implications not just for C. jejuni chemotaxis but for all bacterial chemotaxis.