Literature summary for 3.4.22.47 extracted from

Pomowski, A.; Uson, I.; Nowakowska, Z.; Veillard, F.; Sztukowska, M.N.; Guevara, T.; Goulas, T.; Mizgalska, D.; Nowak, M.; Potempa, B.; Huntington, J.A.; Potempa, J.; Gomis-Rueth, F.X.
Structural insights unravel the zymogenic mechanism of the virulence factor gingipain K from Porphyromonas gingivalis, a causative agent of gum disease from the human oral microbiome (2017), J. Biol. Chem., 292, 5724-5735 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop vapor diffusion method	Porphyromonas gingivalis

Organism

Organism	UniProt	Comment	Textmining
Porphyromonas gingivalis	Q51817	-	-
Porphyromonas gingivalis W83	Q51817	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	gingipain K is secreted as a zymogen. It is inhibited by a pro-domain that is removed during extracellular activation. The isolated 209-residue pro-domain is a boomerang-shaped all-beta protein	Porphyromonas gingivalis

Synonyms

Synonyms	Comment	Organism
KGP	-	Porphyromonas gingivalis

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Release 2023.1 (January 2023)