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Article

The C terminus of SecA is involved in both lipid binding and SecB binding.

The Journal of biological chemistry - 7 Apr 1995

Breukink E, Nouwen N, van Raalte A, Mizushima S, Tommassen J, de Kruijff B

Abstract excerpt

Using C-terminal deletion mutations in secA, we localized the previously proposed (Breukink, E., Keller, R.C. A., and de Kruijff, B. (1993), FEBS Lett. 331, 19-24) second lipid binding site on SecA. Since removal of these residues completely abolished the property of SecA to cause aggregation of negatively charged phosphatidyl-glycerol vesicles, we conclude that the C-terminal 70 amino acid residues of SecA are...

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Identifiers

PMID: 7713885
DOI: 10.1074/jbc.270.14.7902

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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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Research trail→

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The C terminus of SecA is involved in both lipid binding and SecB binding.PMID 7713885Read ↗

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Identification of the preprotein binding domain of SecA.Semantic proximity Read ↗

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

Roles of the C-terminal end of SecY in protein translocation and viability of Escherichia coli.Semantic proximity Read ↗

Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.Semantic proximity Read ↗

Escherichia coli SecA truncated at its termini is functional and dimeric.Semantic proximity Read ↗

Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase.Semantic proximity Read ↗

Roles of SecG in ATP- and SecA-dependent protein translocation.Semantic proximity Read ↗

Dimeric SecA is essential for protein translocation.Semantic proximity Read ↗

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