Literature summary for 3.4.24.29 extracted from

Nickerson, N.N.; Joag, V.; McGavin, M.J.
Rapid autocatalytic activation of the M4 metalloprotease aureolysin is controlled by a conserved N-terminal fungalysin-thermolysin-propeptide domain (2008), Mol. Microbiol., 69, 1530-1543.

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Protein Variants

Protein Variants	Comment	Organism
T85R/L86Y	mutation at the site of autocatalytic activation in the propeptide. Mutation results in secretion of an intact N-terminal propeptide with degradation of the M4 metalloprotease domain. The segment of the fungalysin-thermolysin-propeptide domain promotes intracellular processing of proaureolysin while bestowing a chaperone function	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	mutation T85R/L86Y at the site of autocatalytic activation in the propeptide results in secretion of an intact N-terminal propeptide with degradation of the M4 metalloprotease domain. The fungalysin-thermolysin-propeptide domain promotes intracellular processing of proaureolysin while bestowing a chaperone function	Staphylococcus aureus

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Release 2023.1 (January 2023)