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J. Biol. Chem., Vol. 264, Issue 23, 13579-13585, Aug, 1989
P Vos, G Simons, RJ Siezen and WM de Vos
We have determined the complete nucleotide sequence of the gene for the
cell envelope-located proteinase of Lactococcus lactis SK11. The gene
contains a very AT-rich promoter region followed by the coding sequence of
a protein of 1962 amino acids. Comparison of the NH2-terminal amino acid
sequence of the mature proteinase and the expected primary translation
product of the proteinase gene indicates that the enzyme is probably
synthesized as a pre-pro-protein. This is confirmed by expression studies
of the proteinase gene in Escherichia coli. The amino acid sequence of the
proteinase shows significant homology to a number of serine proteinases of
the subtilisin family. Compared with the related proteinase of L. lactis
Wg2, the proteinase of L. lactis SK11 contains a 60-amino acids duplication
and a total of 44-amino acid substitutions, some of which may account for
the different cleavage specificity of both enzymes. Furthermore, a region
was identified in the Lactococcus proteinase, which shows homology to the
membrane- anchoring domains of a number of proteins from other
Gram-positive bacteria.
Primary structure and organization of the gene for a procaryotic, cell envelope-located serine proteinase
Department of Biophysical Chemistry, Netherlands Institute for Dairy Research (NIZO), Ede.
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