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Molecular characterization of a cell wall‐associated proteinase gene from Streptococcus lactis NCDO763
Author(s) -
Kiwaki M.,
Ikemura H.,
ShimizuKadota M.,
Hiroshima A.
Publication year - 1989
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1989.tb00181.x
Subject(s) - biology , open reading frame , psti , gene , plasmid , peptide sequence , microbiology and biotechnology , genetics , sequence analysis , protease , serine protease , nucleic acid sequence , serine , serine proteinase inhibitors , biochemistry , enzyme , phosphorylation
Summary Streptococcus lactis NCDO763 harbours a plasmid designated pLP763. The cells harbouring pLP763 are able to grow to a higher density in milk because of their proteinase‐positive phenotype (Prt). The 6.2kb HindIII‐Pstl fragment from pLP763 was found to be responsible for the Prt + phenotype. The DNA fragment contains an incomplete large open reading frame (ORF). Further sequence analysis downstream from the Pstl site revealed that the ORF consists of 5706 bases. It was found that the deduced amino acid sequence consisting of 1902 amino acid residues was extremely similar to that of the Wg2 proteinase, a serine protease from Streptococcus cremoris , suggesting that both genes were derived from a common ancestral gene.