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• W2064879781 abstract "The M4 family proteins are common eubacterial metallopeptidases that are involved in a range of functions from nutrient production to pathogenicity. Typically, they consist of a propeptide with inhibitory and chaperone functions and a peptidase unit. The propeptide is cleaved but remains attached until the peptidase is secreted and can be safely activated. Here, we describe a domain in the propeptide that is likely to contain the inhibitory activity, but not the chaperone activity. It is also in many non-peptidase proteins, including Bacillus subtilis YpeB protein – a regulator of SleB spore cortex lytic enzyme – and a large number of eubacterial and archaeal cell-wall-associated and secreted proteins. We propose that it acts as a regulator of peptidase activity in the local environment and also protects the cell from lysis." @default.
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• W2064879781 creator A5051168121 @default.
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• W2064879781 date "2004-04-01" @default.
• W2064879781 modified "2023-10-05" @default.
• W2064879781 title "The PepSY domain: a regulator of peptidase activity in the microbial environment?" @default.
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• W2064879781 doi "https://doi.org/10.1016/j.tibs.2004.02.004" @default.
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