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In prokaryotes, membrane lipoproteins are synthesized with a precursor signal
peptide, which is cleaved by a specific lipoprotein signal peptidase (signal
peptidase II). The peptidase recognizes a conserved sequence and cuts upstream
of a cysteine residue to which a glyceride-fatty acid lipid is attached .
Some of the proteins known to undergo such processing currently include (for
recent listings see [1,2,3]):
Major outer membrane lipoprotein (murein-lipoproteins) (gene lpp).
Escherichia coli lipoprotein-28 (gene nlpA).
Escherichia coli lipoprotein-34 (gene nlpB).
Escherichia coli lipoprotein nlpC.
Escherichia coli lipoprotein nlpD.
Escherichia coli osmotically inducible lipoprotein B (gene osmB).
Escherichia coli osmotically inducible lipoprotein E (gene osmE).
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