PMID:12781516

Citation	Hantke, K (2003) Is the bacterial ferrous iron transporter FeoB a living fossil? Trends Microbiol. 11:192-5
Abstract	The cytoplasmic membrane protein FeoB of Escherichia coli, Helicobacter pylori, Legionella pneumophila and Synechocystis sp. strain PCC 6803 is necessary for Fe(2+) uptake. The C-terminal part of FeoB is predicted to contain 8-12 membrane-spanning helices. The N-terminal domain shows much similarity to eukaryotic and prokaryotic G proteins and, indeed, GTPase activity is necessary for Fe(2+) transport. Four of the five characteristic conserved G protein motifs have been identified in FeoB proteins. Whether FeoB is involved directly, via its Me(2+) binding site, or indirectly in Fe(2+) transport, remains to be investigated.
Links	PubMed
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Biological Transport; Cation Transport Proteins/chemistry; Cation Transport Proteins/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Evolution, Molecular; Ferrous Compounds/metabolism; GTP Phosphohydrolases/chemistry; GTP Phosphohydrolases/physiology; Iron/metabolism; Mutation; Phenotype; Protein Structure, Secondary; Protein Structure, Tertiary/physiology
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