A truncated Bacillus subtilis SecA protein consisting of the N-terminal 234 amino acid residues forms a complex with Escherichia coli SecA51(ts) protein and complements the protein translocation defect of the secA51 mutant.

doi:10.1093/oxfordjournals.jbchem.a124677

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Article

A truncated Bacillus subtilis SecA protein consisting of the N-terminal 234 amino acid residues forms a complex with Escherichia coli SecA51(ts) protein and complements the protein translocation defect of the secA51 mutant.

Journal of biochemistry - 1 Dec 1994

Takamatsu H, Nakane A, Oguro A, Sadaie Y, Nakamura K, Yamane K

Abstract excerpt

Although wild-type Bacillus subtilis SecA barely complements the growth and protein translocation defect of Escherichia coli secA51(ts) at the non-permissive temperature, an N-terminal peptide of B. subtilis SecA complements the defects. To elucidate the mechanism of this complementation, a serie...

Topics

Adenosine Triphosphatases
Amino Acid Sequence
Bacillus subtilis
Bacterial Proteins
Base Sequence
Chromatography, Gel
Chromatography, High Pressure Liquid
Escherichia coli
Escherichia coli Proteins
Genes, Bacterial
Genetic Complementation Test
Membrane Transport Proteins

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Molecular Weight

Mutation

Peptide Fragments

Plasmids

SEC Translocation Channels

Source

Open in PubMed

Identifiers

PMID: 7706219
DOI: 10.1093/oxfordjournals.jbchem.a124677

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7706219-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.