Membrane penicillinase of Bacillus licheniformis 749/C:sequence and possible repeated tetrapeptide structure of the phospholipopeptide region.
The membrane penicillinase (EC 3.5.2.6; penicillin amido-beta-lactamhydrolase) of Bacillus licheniforis 749/C, which appears to be an intermediate in the formation of the exoenzyme, is a phospholipoprotein that carries an NH2-terminal chain of 24 amino acids (only serine, glycine, aspartic acid, asparagine, glutamic acid, and glutamine) and a phosphatidylserine that is not present in the exoenzyme.
D000595:Amino Acid Sequence; D001059:Apoproteins / Q000032:analysis; D001407:Bacillus / Q000201:enzymology* / Q000648:ultrastructure; D002462:Cell Membrane / Q000201:enzymology; D008074:Lipoproteins / Q000032:analysis; D010206:Papain; D010405:Penicillinase / Q000032:analysis* / Q000378:metabolism; D010434:Pepsin A; D010743:Phospholipids / Q000032:analysis
D001059:Apoproteins; D008074:Lipoproteins; D010743:Phospholipids; D010206:Papain; D010434:Pepsin A; D010405:Penicillinase