
Mode of membrane insertion and sequence of a 32‐amino acid peptide stretch of the penicillin‐binding protein 4 of Enterococcus hirae
Author(s) -
Jacques Philippe,
El Kharroubi Aboubaker,
Beeumen Jozef,
Piras Grazielle,
Coyette Jacques,
Ghuysen JeanMarie
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04851.x
Subject(s) - enterococcus hirae , peptide , penicillin binding proteins , peptide sequence , n terminus , biochemistry , amino acid , chemistry , sequence (biology) , enterococcus , biology , penicillin , antibiotics , gene
Analysis of water‐soluble derivatives of the Enterococcus hirae 75‐kDa membrane‐bound penicillin‐binding protein 4 (PBP4) has yielded the amino acid sequence of a 32‐amino acid polypeptide stretch. This peptide is similar to peptide segments known to occur in the N‐terminal domain of high‐ M r PBPs of class B. The E. hirae PBP4 probably belongs to the same class. It is anchored in the membrane at the N‐terminus of the polypeptide chain.