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Article

Roles of the conserved cytoplasmic region and non-conserved carboxy-terminal region of SecE in Escherichia coli protein translocase.

Journal of biochemistry - 1 Jun 1996

Kontinen V P, Yamanaka M, Nishiyama K, Tokuda H

Abstract excerpt

SecE, an essential membrane component of the Escherichia coli protein translocase, consists of 127 amino acid residues. Only a part of the second putative cytoplasmic region comprising some 13 residues is essential for the SecE function as long as the proper topological arrangement is retained. The Trp84 and Pro85 residues of this region are conserved in all eubacterial SecE homologues. The conservation of...

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Identifiers

PMID: 8827448
DOI: 10.1093/oxfordjournals.jbchem.a021358

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Roles of the conserved cytoplasmic region and non-conserved carboxy-terminal region of SecE in Escherichia coli protein translocase.PMID 8827448Read ↗

Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region.Semantic proximity Read ↗

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Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states.Semantic proximity Read ↗

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Importance of transmembrane segments in Escherichia coli SecY.Semantic proximity Read ↗

A SecE mutation that modulates SecY-SecE translocase assembly, identified as a specific suppressor of SecY defects.Semantic proximity Read ↗

Protein translocation functions of Escherichia coli SecY: in vitro characterization of cold-sensitive secY mutants.Semantic proximity Read ↗

An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY.Semantic proximity Read ↗

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