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Fungalysin/Thermolysin Propeptide Motif
This motif is found in both the bacterial M4 peptidase propeptide and the fungal M36 propeptide. Its exact function is not clear, but it is likely to either inhibit the peptidase, so as to prevent its premature activation, or has a chaperone activity. Both of these roles have been ascribed to the M4 and M36 propeptides ([1], [2]). [1]. 12589825. General function of N-terminal propeptide on assisting protein. folding and inhibiting catalytic activity based on observations. with a chimeric thermolysin-like protease.. Tang B, Nirasawa S, Kitaoka M, Marie-Claire C, Hayashi K;. Biochem Biophys Res Commun 2003;301:1093-1098.. [2]. 8636020. Specific inhibition of mature fungal serine proteinases and. metalloproteinases by their propeptides.. Markaryan A, Lee JD, Sirakova TD, Kolattukudy PE;. J Bacteriol 1996;178:2211-2215. (from Pfam)
PepSY domain-containing protein
This region is likely to have an protease inhibitory function (personal obs:C Yeats). This model is likely to miss some members of this family as the separation from signal to noise is not clear. The name is derived from Peptidase & Bacillus subtilis YPEB. [1]. 7674922. Evolutionary families of metallopeptidases.. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228.. [2]. 15124630. The PepSY domain: a regulator of peptidase activity in the. microbial environment?.. Yeats C, Rawlings ND, Bateman A;. Trends Biochem Sci 2004;29:169-172.. [3]. 15583150. Identification of residues in the Pseudomonas aeruginosa. elastase propeptide required for chaperone and secretion. activities.. McIver KS, Kessler E, Ohman DE;. Microbiology 2004;150:3969-3977. (from Pfam)
Thermolysin metallopeptidase, catalytic domain
M4 family metallopeptidase
M4 family metalopeptidase is a zinc metallopeptidase that contains an HEXXH motif, where the histidines are zinc ligands and the glutamate is an active site residue, preferably cleaving Xaa+Yaa, in which Xaa is a hydrophobic residue and Yaa is Leu, Phe, Ile, or Val
neutral metalloprotease NprE
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