Is the bacterial ferrous iron transporter FeoB a living fossil?
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.
Hantke
Klaus
K
Mikrobiologie/Membranphysiologie, Universität Tübingen, Auf der Morgenstelle 28, Tübingen, Germany. hantke@uni-tuebingen.de
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport; D027682:Cation Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D005296:Ferrous Compounds / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000502:physiology; D007501:Iron / Q000378:metabolism*; D009154:Mutation; D010641:Phenotype; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary / Q000502:physiology
D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D029968:Escherichia coli Proteins; C470580:FeoB protein, E coli; C414315:FeoB protein, Helicobacter pylori; D005296:Ferrous Compounds; D007501:Iron; D020558:GTP Phosphohydrolases