Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site.

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Article

Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site.

The Journal of biological chemistry - 25 Feb 1990

Fikes J D, Barkocy-Gallagher G A, Klapper D G, Bassford P J

Abstract excerpt

Comparative analyses of a number of secretory proteins processed by eukaryotic and prokaryotic signal peptidases have identified a strongly conserved feature regarding the residues positioned -3 and -1 relative to the cleavage site. These 2 residues of the signal peptide are thought to constitute a recognition site for the processing enzyme and are usually amino acids with small, neutral side chains. It was shown...

Topics

ATP-Binding Cassette Transporters
Amino Acid Sequence
Base Sequence
Carrier Proteins
Endopeptidases
Escherichia coli
Escherichia coli Proteins
Maltose
Maltose-Binding Proteins
Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Monosaccharide Transport Proteins

Mutation

Oligonucleotide Probes

Protein Precursors

Protein Processing, Post-Translational

Serine Endopeptidases

Source

Open in PubMed

Identifiers

PMID: 2406254

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2406254-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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