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Article

Essential cytoplasmic domains in the Escherichia coli TatC protein.

The Journal of biological chemistry - 22 Mar 2002

Allen Stuart C H, Barrett Claire M L, Ray Nicola, Robinson Colin

Abstract excerpt

The twin-arginine translocation (Tat) system mediates the transport of proteins across the bacterial plasma membrane and chloroplast thylakoid membrane. Operating in parallel with Sec-type systems in these membranes, the Tat system is completely different in both structural and mechanistic terms, and is uniquely able to catalyze the translocation of fully folded proteins across coupled membranes. TatC is an...

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Identifiers

PMID: 11781311
DOI: 10.1074/jbc.M109135200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Essential cytoplasmic domains in the Escherichia coli TatC protein.PMID 11781311Read ↗

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Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.Semantic proximity Read ↗

A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins.Semantic proximity Read ↗

A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes.Semantic proximity Read ↗

Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein.Semantic proximity Read ↗

Overlapping functions of components of a bacterial Sec-independent protein export pathway.Semantic proximity Read ↗

Role of the Escherichia coli Tat pathway in outer membrane integrity.Semantic proximity Read ↗

The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Semantic proximity Read ↗

The entire N-terminal half of TatC is involved in twin-arginine precursor binding.Semantic proximity Read ↗

Twin arginine translocation (Tat)-dependent export in the apparent absence of TatABC or TatA complexes using modified Escherichia coli TatA subunits that substitute for TatB.Semantic proximity Read ↗

Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.Semantic proximity Read ↗

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