The structure of signal peptides from bacterial lipoproteins.
Statistical analysis of lipoprotein and non-lipoprotein signal peptides reveals that the two classes differ significantly only in the region close to the signal peptidase cleavage site. This region is apolar and has the consensus sequence LA(G,A) decreases C in the lipoproteins, but is polar and has small, uncharged residues in positions -3 and -1 in the non-lipoproteins. A simple search for matches to the lipoprotein consensus cleavage site suffices to discriminate between the two groups with close to 100% reliability.
von Heijne
G
G
Department of Molecular Biology, Karolinska Institutet, Huddinge Hospital, Sweden.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D003627:Data Interpretation, Statistical; D010450:Endopeptidases; D006090:Gram-Negative Bacteria; D006094:Gram-Positive Bacteria; D008074:Lipoproteins / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins; D008722:Methods; D008969:Molecular Sequence Data; D015394:Molecular Structure; D021382:Protein Sorting Signals / Q000235:genetics / Q000378:metabolism; D012697:Serine Endopeptidases
D001426:Bacterial Proteins; D008074:Lipoproteins; D008565:Membrane Proteins; D021382:Protein Sorting Signals; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase