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Article

Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box.

Journal of bacteriology - 1 Mar 2003

Ogierman Monica, Braun Volkmar

Abstract excerpt

Both induction of transcription of the ferric citrate transport genes and transport of ferric citrate by the Escherichia coli outer membrane receptor FecA require energy derived from the proton motive force (PMF) of the inner membrane. The energy is transduced to FecA by the inner membrane comple...

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Identifiers

PMID: 12618451
DOI: 10.1128/JB.185.6.1870-1885.2003
PMCID: PMC150147

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-12618451-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box.PMID 12618451Read ↗

Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions.Semantic proximity Read ↗

Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA.Semantic proximity Read ↗

Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli.Semantic proximity Read ↗

Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains.Semantic proximity Read ↗

Defined inactive FecA derivatives mutated in functional domains of the outer membrane transport and signaling protein of Escherichia coli K-12.Semantic proximity Read ↗

Control of the ferric citrate transport system of Escherichia coli: mutations in region 2.1 of the FecI extracytoplasmic-function sigma factor suppress mutations in the FecR transmembrane regulatory protein.Semantic proximity Read ↗

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The beta-barrel domain of FhuADelta5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli.Semantic proximity Read ↗

Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein.Semantic proximity Read ↗

Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport.Semantic proximity Read ↗

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