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The ATP‐dependent CodWX (HslVU) protease in Bacillus subtilis is an N‐terminal serine protease
Author(s) -
Kang Min Suk,
Lim Byung Kook,
Seong Ihn Sik,
Seol Jae Hong,
Tanahashi Nobuyuki,
Tanaka Keiji,
Chung Chin Ha
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.4.734
Subject(s) - library science , metropolitan area , biological sciences , political science , medicine , biology , microbiology and biotechnology , computer science , pathology
HslVU is a two‐component ATP‐dependent protease, consisting of HslV peptidase and HslU ATPase. CodW and CodX, encoded by the cod operon in Bacillus subtilis , display 52% identity in their amino acid sequences to HslV and HslU in Escherichia coli , respectively. Here we show that CodW and CodX can function together as a new type of two‐component ATP‐dependent protease. Remarkably, CodW uses its N‐terminal serine hydroxyl group as the catalytic nucleophile, unlike HslV and certain β‐type subunits of the proteasomes, which have N‐terminal threonine functioning as an active site residue. The ATP‐dependent proteolytic activity of CodWX is strongly inhibited by serine protease inhibitors, unlike that of HslVU. Replacement of the N‐terminal serine of CodW by alanine or even threonine completely abolishes the enzyme activity. These results indicate that CodWX in B.subtilis represents the first N‐terminal serine protease among all known proteolytic enzymes.