The peptidoglycan-associated lipoprotein (PAL) of the Proteus mirabilis outer membrane: characterization of the peptidoglycan-associated region of PAL.
The peptidoglycan-associated lipoprotein (PAL) is present in the cell envelope in a form closely, but not covalently, associated with peptidoglycan in various Gram-negative bacteria. When the cell envelope or the isolated peptidoglycan-PAL complex from Proteus mirabilis, in which PAL maintains the interaction with peptidoglycan, was digested with trypsin, a polypeptide fragment with molecular weight 11,000 (11 K fragment) was obtained. However, when isolated PAL or the 11 K-fragment which had been dissociated from peptidoglycan was treated with trypsin, they were further digested. The 11 K-fragment maintained essentially the same tight interaction with peptidoglycan as intact PAL. These results indicate that the 11 K-fragment is probably derived from the peptidoglycan-associated region of the PAL molecule. The purified 11 K-fragment contained neither covalently-linked fatty acid nor glycerylcysteine, which are known to be present at the N-terminus of PAL. The N-terminal sequence of the 11 K-fragment was also determined.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001425:Bacterial Outer Membrane Proteins; D002473:Cell Wall / Q000032:analysis; D029968:Escherichia coli Proteins; D008074:Lipoproteins / Q000378:metabolism*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010457:Peptidoglycan / Q000378:metabolism*; D011509:Proteoglycans; D011513:Proteus mirabilis / Q000032:analysis*; D014357:Trypsin
D000596:Amino Acids; D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C031163:ExcC protein, E coli; D008074:Lipoproteins; D010446:Peptide Fragments; D010457:Peptidoglycan; D011509:Proteoglycans; C069988:PplA protein, Legionella pneumophila; D014357:Trypsin