The Complete Amino Acid Sequence of the Acyl Carrier Protein of Escherichia coli

Abstract

The complete amino acid sequence of the acyl carrier protein (ACP) from Escherichia coli has been established. It contains 77 residues with NH2-terminal serine and COOH-terminal alanine. The pantotheine prosthetic group of ACP is attached covalently to the hydroxyl group of serine at residue 36, which is 1 of 3 seryl residues in the molecule. This unique sequence was deduced by sequence analysis of the tryptic, peptic, and thermolysin peptides isolated from enzymic hydrolysates of ACP as described earlier. Important overlaps in sequence were also obtained by partial sequence analysis of one of the two unique peptides formed on cleavage of ACP with CNBr, and by sequence analysis of a single tryptic peptide isolated from tryptic digests of ACP modified at its single arginyl residue with 1,2-cyclohexanedione.