The type VIIb protein secretion system (T7SSb) is found inBacillota(firmicute) bacteria and has been shown to mediate interbacterial competition. EssC is a membrane-bound ATPase that is a critical component of the T7SSb and plays a key role in substrate recognition. Prior analysis of available genome sequences of the foodborne bacterial pathogenListeria monocytogeneshas shown that although the T7SSb was encoded as part of the core genome, EssC could be found as one of seven different sequence variants. While each sequence variant was associated with a specific suite of candidate substrate proteins encoded immediately downstream ofessC, many LXG-domain proteins were encoded across multipleessCsequence variants. Here, we have extended this analysis using a diverse collection of 37 930L.monocytogenesgenomes. We have identified a rare eighth variant of EssC present in tenL. monocytogeneslineage III genomes. These genomes also encode a large toxin of the rearrangement hotspot (Rhs) repeat family adjacent toessC8, along with a probable immunity protein and three small accessory proteins. We have further identified nine novel LXG-domain proteins, and four additional chromosomal hotspots acrossL. monocytogenesgenomes where LXG proteins can be encoded. The eightL. monocytogenesEssC variants were also found in otherListeriaspecies, with additional novel EssC types also identified. Across the genus, species frequently encoded multiple EssC types, indicating that T7SSb diversity is a primary feature of the genusListeria.