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The envelope of Escherichia coli consists of two distinct membranes, the outer membrane and the cytoplasmic membrane. The space between the two membranes is called the periplasmic space, and each fraction contains its own specific proteins. In this review, it is discussed how proteins are localized in their final locations in the envelope. Proteins localized in the outer membrane and the periplasmic space as well as transmembranous proteins in the cytoplasmic membranes appear to be produced from their precursors which have peptide extensions of about 20 amino acid residues at the amino terminal ends. General features for the peptide extension are deduced from the known sequences of the peptide extensions, and, based on their known properties, a hypothesis (loop model) is proposed to explain the possible functions of the peptide extension during the mechanism of secretion across the cytoplasmic membrane.
Inouye et al. (1980) studied this question.