Abstract
Bacteria commonly utilise a unique type of transporter, called Feo, to specifically acquire the ferrous (Fe2+) form of iron from their environment. Enterobacterial Feo systems are composed of three proteins: FeoA, a small, soluble SH3-domain protein probably located in the cytosol; FeoB, a large protein with a cytosolic N-terminal G-protein domain and a C-terminal integral inner-membrane domain containing two 'Gate' motifs which likely functions as the Fe2+ permease; and FeoC, a small protein apparently functioning as an [Fe-S]-dependent transcriptional repressor. We provide a review of the current literature combined with a bioinformatic assessment of bacterial Feo systems showing how they exhibit common features, as well as differences in organisation and composition which probably reflect variations in mechanisms employed and function.
Original language | English |
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Pages (from-to) | 143-157 |
Number of pages | 15 |
Journal | BioMetals |
Volume | 19 |
Issue number | 2 |
DOIs | |
Publication status | Published - Apr 2006 |
Externally published | Yes |
Keywords
- DtxR
- FeoA
- FeoB
- FeoC
- G-protein
- Gate motif
- Manganese
- Meo
- MntR
- SH3
- Transport