Campylobacter jejuni colonization and pathogenicity require the bacteria to sense the chemicals in its environment and move toward the target host tissues in order to cause disease. The first and the most critical step in this process is initiated by membrane-bound sensory proteins, chemoreceptors, which recognise chemical signals and trigger a response directing a cell to move toward an attractant or away from a repellent, as well as direct the microbe toward a susceptible host cell. Here, we illustrate that the molecule - sensing repertoire of C. jejuni chemoreceptor family Tlp2, Tlp3 and Tlp4 includes sugars and amino- and organic acids, commonly found in animal intestinal tract. We demonstrate that the receptors sense this wide variety of chemicals via a single binding pocket with high and low affinity binding sites where one or more molecules can be bound at the same time. We also reveal that Tlp2, Tlp3 and Tlp4 receptors may have arisen through gene duplications followed by a divergent evolutionary drift. Diverse sensory repertoire could provide C. jejuni with the ability to modulate responses to attractant and repellent signals and allow adaptation for host-pathogen interactions.