Role of C-terminal domains in surface attachment of the fructosyltransferase of Streptococcus salivarius ATCC 25975.
The cell-associated beta-D-fructosyltransferase of Streptococcus salivarius, which is devoid of the cell wall anchoring motif, LPXTG, is released on exposure to its substrate, sucrose. Deletions within the C terminus of the enzyme implicated both the hydrophobic and the proline-glycine-serine-threonine-rich wall-associated domain in stabilizing the enzyme on the cell surface.
Rathsam
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C
Institute of Dental Research, Surry Hills, New South Wales 2010, Australia.
Jacques
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D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D004795:Enzyme Stability; D006602:Hexosyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D011480:Protease Inhibitors / Q000494:pharmacology; D017384:Sequence Deletion; D013291:Streptococcus / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins
D006602:Hexosyltransferases; D011480:Protease Inhibitors; C021451:inulosucrase; D001426:Bacterial Proteins