Helicobacter pylori (H. pylori) is a clinically significant gastric pathogen associated with a range of gastric conditions including peptic ulcer disease and gastric cancer, and its eradication is increasingly compromised by rising antimicrobial resistance (AMR). As treatment failure rates increase, there is growing interest in bacteriophage-derived lytic enzymes as alternative or adjunct antimicrobial strategies. However, the functional potential of prophage-encoded lysis-associated genes in H. pylori remains poorly characterised. In this research, we analysed whole-genome sequences from 33 clinical H. pylori isolates obtained from 18 patients in the United Kingdom to analyse prophage content and identify associated lysis genes. 16 prophage regions were identified, of which nine encoded lysis-associated genes, including 16 predicted endolysins and two holins. Several endolysins contained conserved catalytic domains linked to peptidoglycan degradation, including members of the peptidase M23 and S26 families, consistent with potential roles in peptidoglycan degradation, although functional activity remains to be experimentally confirmed. Sequence variation in endolysins was observed within individual strains harbouring multiple prophages, indicating a potential reservoir of functionally diverse lytic enzymes. Preliminary experimental work involving cloning and expression of selected lysis-associated genes did not demonstrate clear antibacterial activity against H. pylori using crude extracts, likely reflecting limitations in protein purification and assay optimisation. Overall, these findings highlight substantial diversity in prophage-encoded lysis-associated genes within clinical H. pylori isolates and support their potential as a source of novel antimicrobial tools. Further functional characterisation will be essential to assess their applicability in addressing AMR in this pathogen.