Journal
FEBS LETTERS
Volume 584, Issue 21, Pages 4419-4425Publisher
WILEY
DOI: 10.1016/j.febslet.2010.09.049
Keywords
Bacillus intermedius; Metalloproteinase; ADAM-like proteinase; HEXXHXXGXXH motif; Molecular cloning; Gene expression; Protein purification
Funding
- Science and teaching program of innovative Russia
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The mprBi gene from Bacillus intermedius 3-19 encoding a novel secreted metalloproteinase was identified. The mpriBi gene was expressed in an extracellular proteinase-deficient Bacillus subtilis BG 2036 strain and the corresponding protein was characterized biochemically. The 19 kDa MprBi protein was purified to homogeneity and sequenced by mass spectroscopy and Edman degradation methods. Amino acid sequence analysis of MprBi identified an active site motif HEYGHNFGLPHD and a conserved structural component Met-turn, both of which are unique features of the metzincin clan. Furthermore, MprBi harbors a number of distinct sequence elements characteristic of proteinase domains in eukaryotic adamalysins. We conclude that MprBi and similar proteins from other Bacillus species form a novel group of metzincin metalloproteinases in prokaryotes. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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