{'fraction_non_alphanumeric': 0.027939464493597205, 'fraction_numerical': 0.025611175785797437, 'mean_word_length': 5.825396825396825, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Characterization of a Porphyromonas gingivalis gene prtK that encodes a lysine-specific cysteine proteinase and three sequence-related adhesins.

Porphyromonas gingivalis extracellular arginine- and lysine-specific proteinases have been implicated as major virulence factors in the development of adult periodontitis. We have previously purified a 48-kDa lysine-specific cysteine proteinase, designated PrtK48, from a P. gingivalis W50 cell-associated multiprotein complex. PrtK48 was non-covalently associated with three sequence-related adhesins designated PrtK39, PrtK15 and PrtK44 in the multiprotein complex. In this study we cloned and characterized the gene, designated prtK, that encodes a polyprotein that is post-translationally processed to yield the Lys-specific proteinase PrtK48 and the three sequence-related adhesins PrtK39, PrtK15 and PrtK44.