A peptidoglycan binding domain in the porin-associated protein (PAP) of Rhodospirillum rubrum FR1.
The porin-associated protein of Rhodospirillum rubrum FR1 was found to contain a peptidoglycan binding motif. A partial fragment of 179 amino acids, obtained by cleavage of PAP with trypsin, Asp-N protease, and CNBr, was sequenced. Substantial sequence homology was found of the C-terminal part (residues 126-179) of porin-associated protein with OmpA, the peptidoglycan-associated lipoprotein of several bacteria, protein F of Pseudomonas aeruginosa, and PIII of Neisseria gonorrhoeae, the latter being also a porin-associated protein. The 179 amino acid fragment comprised about 67% of the mass spectrometrically determined total mass of PAP of 27850 Da.
Neumann
U
U
Institut für Biologie II, Mikrobiologie, der Albert-Ludwigs-Universität, Freiburg, Germany. uneumann@sun2.ruf.uni-freiburg.de
Schiltz
E
E
Stahl
B
B
Hillenkamp
F
F
Weckesser
J
J
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites / Q000235:genetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics; D010457:Peptidoglycan / Q000378:metabolism*; D018272:Porins / Q000235:genetics / Q000378:metabolism*; D012247:Rhodospirillum rubrum / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D010446:Peptide Fragments; D010457:Peptidoglycan; D018272:Porins; C051591:Rmp protein, Neisseria