TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
2.A.108.1: The Oxidase-dependent Fe2+ Transporter (OFeT) Family | ||||
2.A.108.1.1 | High-affinity oxidase-dependent plasma membrane Fe2+-Fe3+ uptake transporter, Ftr1 of 404 aas and 7 TMSs in a 3 + 3 + 1 TMS arrangement with the N-terminus out and the C-termius in (Severance et al. 2004). There are two REXLE (Arg-Glu-Xaa-Leu-Glu) motifs in transmembrane domains 1 and 4, both essential for transport activity, implying the presence of a 3 TMS repeat ((Severance et al. 2004)). Ftr1 may be a "transceptor", combining transport and receptor functions (Diallinas 2017). | Eukaryota |
Fungi, Ascomycota | Fet3 and Ftr1 of Saccharomyces cerevisiae Fet3 (aka Fet3p) (multicopper ferrooxidase) Ftr1 (Fe3+ transporter) |
2.A.108.1.2 | Iron-repressible Fe2+ uptake porter, FTR1 (Ziegler et al. 2011) | Eukaryota |
Fungi, Ascomycota | Ftr1 of Candida albicans |
2.A.108.1.3 | Iron-inducible Fe2+ uptake porter, FTR2 | Eukaryota |
Fungi, Ascomycota | Ftr2 of Candida albicans |
2.A.108.1.4 | High-affinity oxidase-dependent vacuolar Fe2+-Fe3+ uptake transporter (Singh et al. 2006) | Eukaryota |
Fungi, Ascomycota | Fet5p and Fth1p of Saccharomyces cerevisiae Fet5p (multicopper ferrooxidase) (NP_116612) Fth1p (Fe3+ transporter) (NP_009766) |
2.A.108.1.5 | High-affinity oxidase-dependent plasma membrane Fe2+-Fe3+ uptake transporter, Fio1/Fip1 (Frp1) (Singh et al., 2006). Metalloreductase responsible for reducing extracellular iron and copper prior to import. It catalyzes the reductive uptake of Fe3+-salts and Fe3+ bound to catecholate or hydroxamate siderophores. Fe3+ is reduced to Fe2+, which then dissociates from the siderophore and can be imported by the high-affinity Fe2+ transport complex in the plasma membrane. Fio1 is a multicopper oxidase that contains three cupredoxin domains with eleven candidate iron-binding ligands, whereas Frp1 harbors a ferric reductase domain with three-candidate heme-binding ligands. The complex also participates in Cu2+ reduction and Cu+ uptake (Ahmad et al. 2022). | Eukaryota |
Fungi, Ascomycota | Fio1 and Fip1 of Schizosaccharomyces pombe Fio1 (multicopper ferrooxidase) (Q09920) Fip1 (Fe3+ transporter) (Q09919) |
2.A.108.1.6 | Iron transporter, Ftr1 (541 aas) (La Fontaine et al., 2002). FTR1, like its orthologue in S. cerevisiae (9.A.10.1.1), has an exocytoplasmic iron channeling motif and two potential iron permeation motifs in membrane-spanning regions (Terzulli and Kosman 2010). | Eukaryota |
Viridiplantae, Chlorophyta | Ftr1 of Chlamydomonas reinhardtii (AAM45938) |
2.A.108.1.7 | The Ftr1/Fet3 high-affinity iron uptake system (Larrondo et al., 2007) | Eukaryota |
Fungi | Ftr1/Fet3 of Phanerochaete chrysosporium Ftr1 (Q1P9T0) Fet3 (Q1P9T1) |
2.A.108.1.8 | High affinity iron permease, CaFtr1 (Jung et al. 2008) | Eukaryota |
Fungi, Basidiomycota | CaFtr1 of Cryptococcus neoformans (Q5KJQ5) |
2.A.108.2.1 | The lead (Pb2+) uptake porter, PbrT | Bacteria |
Pseudomonadota | PbrT of Ralstonia metallidurans CH34 (gbCAC28871) |
2.A.108.2.2 | The high-affinity oxidase-dependent iron (ferric/ferrous) transporter, FTR-ChpA | Bacteria |
Pseudomonadota | FTR-ChpA of Brucella melitensis FTR (AAL54125) |
2.A.108.2.3 | The acid-induced, low pH, ferrous iron (Fe2+) uptake transporter, EfeUOB (YcdN); cryptic in E. coli K12 (Cao et al. 2007; Grosse et al., 2006) | Bacteria |
Pseudomonadota | EfeUOB of E. coli O157:H5 EfeU - P75901 EfeO (periplasmic cupredoxin domain containing protein) - P0AB24 EfeB (peroxidase) - P31545 |
2.A.108.2.4 | The Ftr1 (integral membrane transporter)/ P19 (periplasmic iron binding protein) iron uptake system. P19 has distinct copper and iron binding sites and exhibits an immunoglobulin-like fold (Chan et al., 2010). | Bacteria |
Campylobacterota | Ftr1/P19 of Campylobacter jejuni Ftr1 (Q5HSD5) P19 (Q0P7X0) |
2.A.108.2.5 | Bacteria |
Bacillota | EfeU of Bacillus subtilis | |
2.A.108.2.6 | High affinity Fe2+/Pb2+ permease-like protein. | Bacteria |
Chloroflexota | Permease of Thermobaculum terrenum |
2.A.108.2.7 | Pb2+ uptake porter of 643 aas, PbtT or FTR1 (Hložková et al. 2013). | Bacteria |
Pseudomonadota | PbtT of Achromobacter xylosoxidans |
2.A.108.2.8 | Ftr1 protein of 276 aas and 8 TMSs | Archaea |
Thermoproteota | Ftr1 protein of Aeropyrum pernix |
2.A.108.2.9 | Siderophore-independent iron uptake porter, FtrCAB: FtrC (280 aas, 7 TMSs)/FtrA (183 aas; 1 TMS)/FtrB (110 aas, 0 TMSs) (Mathew et al. 2014). Functions with FtrD, an iron-sulfur cluster-containing ferredoxin of 465 aas. | Bacteria |
Pseudomonadota | FtrCAB of Burkholderia cenocepacia |
2.A.108.2.10 | Dipartite iron uptake system, FetM (646 aas; 8 TMSs in a 1 + 7 TMS arrangement)/FetP (a periplasmic protein that enhances iron uptake by FetM) (Koch et al. 2011). FetP binds Cu2+ and Mn2+ at two different sites, 1.3 Å apart, in this homodimeric protein, and the 3-d structure with Cu2+ bound to each of the two subunits reveals different geometries at the two sites. FetMP may be an iron permease with an iron scavenging function, and possibly also an iron reducing function (Koch et al. 2011). | Bacteria |
Pseudomonadota | FetMP of E. coli |
2.A.108.2.11 | Putative heavy metal transporter, Ftr1/Tp34 or Tpd, (TP0972/TP0971). Ftr1 has 448 aas with 9 TMSs while Tp34 has 204 aas with 1 N-terminal TMSs. This antigen is a pathogen-specific membrane immunogen. This periplasmic dimeric protein binds human lactoferrin with submicromolar affinity with a stoichiometry of 2:1 (Deka et al. 2007). It's 3-d structure (1.9 Å resolution) reveals two metal binding sites per monomer with zinc bound to both sites (Deka et al. 2007). | Spirochaetota | Ftr1/Tdp of Treponema pallidum | |
2.A.108.3.1 | Hypothetical protein of 208 aas | Archaea |
Thermoproteota | HP of Sulfolobus islandicus |
2.A.108.3.2 | Manganese ion transporter, MntH of 250 aas and 6 - 7 TMSs. | Bacteria |
Pseudomonadota | MntH of Rhizobium leguminosarum |
2.A.108.3.3 | Hypothetical protein | Archaea |
Thermoproteota | HP of Sulfolobus acidocaldarius |