Phenotypic characterization of the foldase homologue PrsA inStreptococcus mutans
نویسندگان
چکیده
منابع مشابه
Dimeric Structure of the Bacterial Extracellular Foldase PrsA.
Secretion of proteins into the membrane-cell wall space is essential for cell wall biosynthesis and pathogenicity in Gram-positive bacteria. Folding and maturation of many secreted proteins depend on a single extracellular foldase, the PrsA protein. PrsA is a 30-kDa protein, lipid anchored to the outer leaflet of the cell membrane. The crystal structure of Bacillus subtilis PrsA reveals a centr...
متن کاملThe peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis.
The prsA-like gene from Lactococcus lactis encoding its single homologue to PrsA, an essential protein triggering the folding of secreted proteins in Bacillus subtilis, was characterized. This gene, annotated pmpA, encodes a lipoprotein of 309 residues whose expression is increased 7- to 10-fold when the source of nitrogen is limited. A slight increase in the expression of the PrsA-like protein...
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ژورنال
عنوان ژورنال: Molecular Oral Microbiology
سال: 2012
ISSN: 2041-1006
DOI: 10.1111/omi.12014