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

doi:10.1007/BF00266243

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Article

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

Molecular & general genetics : MGG - 1 Apr 1992

Köster W, Böhm B

Abstract excerpt

A region of substantial homology, comprising 32 amino acids around a highly conserved glycine residue, is located near the C-terminal ends of the hydrophobic Fhu, Fec, Fep, Fat, and Btu transport proteins involved in the uptake of ferrisiderophores and vitamin B12 into Escherichia coli and Vibrio anguillarum. Furthermore, a region similar in location and sequence containing an invariant glycine at an equivalent...

Topics

Amino Acid Sequence
Anti-Bacterial Agents
Base Sequence
Biological Transport
Carrier Proteins
Escherichia coli
Escherichia coli Proteins
Ferric Compounds
Ferrichrome
Genotype
Glycine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Hydroxamic Acids

Kinetics

Membrane Proteins

Membrane Transport Proteins

Molecular Sequence Data

Mutagenesis, Site-Directed

Oligodeoxyribonucleotides

Source

Open in PubMed

Identifiers

PMID: 1588908
DOI: 10.1007/BF00266243

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1588908-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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