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The sites of three closely linked <jats:italic>prs<\/jats:italic> mutations (<jats:italic>prs\u20103, prs\u201029 and prs\u201040<\/jats:italic>) were found to reside in a 5.3kb DNA fragment, which also complemented the secretion defect in <jats:italic>prs\u20103<\/jats:italic> and <jats:italic>prs\u201029<\/jats:italic> mutants. Partial sequencing of the fragment showed that these three mutations affect one distinct gene (<jats:italic>prs A<\/jats:italic>) encoding a putative protein of 292 amino acids (33 kDa). Sequence analysis Indicated the <jats:italic>PrsA<\/jats:italic> protein to be a lipoprotein located outside the cytoplasmic membrane. Thirty percent identity was shown to the PrtM protein of Lactococcus lactis, which is involved in the maturation of an exported proteinase. The phenotypes of <jats:italic>prsA<\/jats:italic> mutants and the structural similarity of PrsA with PrtM suggest that PrsA may have a novel function at a late phase in protein export.<\/jats:p>","DOI":"10.1111\/j.1365-2958.1991.tb01901.x","type":"journal-article","created":{"date-parts":[[2006,10,27]],"date-time":"2006-10-27T22:01:48Z","timestamp":1161986508000},"page":"1273-1283","source":"Crossref","is-referenced-by-count":105,"title":["A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export"],"prefix":"10.1111","volume":"5","author":[{"given":"V. 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