| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
2.A.104.1.1 | The L-alanine exporter, AlaE (YgaW) of 149 aas and 4 TMSs. (In the DUF1144 or PF06610 superfamily) (Hori et al., 2011). Two charged residues are essential for it's efflux activity (Kim et al. 2016). AlaE is the physiologically most relevant exporter for L-alanine in E. coli. AlaE forms homo-oligomers, and the GxxxG motif in the TMS4 region plays an essential role in AlaE activity but not in AlaE oligomer formation (Ihara et al. 2022). | Bacteria |
Pseudomonadota | AlaE of E. coli (A8ANM6) |
|
2.A.104.1.2 | AlaE homologue of 149aas and 4 TMSs. There is a duplicated 2 TMS repeat unit, and immediately following both TMSs 2 and 4, there is a conserved motif, RPYG-W found in both halves of the protein at residue numbers 55 and 122 respectively. Thus, AlaE homologues arose by an intergenic duplication event. | Bacteria |
Pseudomonadota | AlaE homologue of Pelagibacterium halotolerans (G4R961) |
|
2.A.104.2.1 | Hypothetical protein (77aas; 2 TMSs). Resembles residues 72-149 (second half) of AlaE. Could be a fragment of the full length protein. | Archaea |
Thermoproteota | HP of an uncultured crenarchaeote (H5SVY7) |
|
2.A.104.3.1 | AlaE homologue of 159 aas and 3 or 4 TMSs (KKS95321.1) | Bacteria |
Candidatus Giovannonibacteria | AlaE of Parcubacteria (Giovannonibacteria) bacterium (KKS95321.1) |
|
2.A.104.3.2 | AlaE homologue of 150 aas and 4 TMSs (KKP64473.1). | Bacteria |
Candidatus Nomurabacteria | AlaE of Parcubacteria (Nomurabacteria) bacterium GW2011_GWF2_35_12 (KKP64473.1) |