Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo.

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Article

Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo.

The Journal of biological chemistry - 25 Feb 1993

Klose M, Schimz K L, van der Wolk J, Driessen A J, Freudl R

Abstract excerpt

The SecA protein is a major component of the cellular machinery that mediates the translocation of proteins across the Escherichia coli plasma membrane. The secA gene from Bacillus subtilis was cloned and expressed in E. coli under the control of the lac or trc promoter. The temperature-sensitive...

Topics

Adenosine Triphosphatases
Adenosine Triphosphate
Amino Acid Sequence
Bacillus subtilis
Bacterial Outer Membrane Proteins
Bacterial Proteins
Base Sequence
Binding Sites
Biological Transport
Catalysis
DNA, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Escherichia coli

Escherichia coli Proteins

Genetic Complementation Test

Lysine

Membrane Transport Proteins

Molecular Sequence Data

Mutation

Source

Open in PubMed

Identifiers

PMID: 8440733

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8440733-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo.PMID 8440733Read ↗

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