TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
---|---|---|---|---|
2.A.42.1.1 | Tyrosine permease | Bacteria |
Pseudomonadota | TyrP of E. coli (P0AAD4) |
2.A.42.1.2 | High affinity (3 μM tryptophan permease, Mtr. Also transports indole. It functions to scavenge trace amounts of tryptophan in the medium for protein synthesis when concentrations are very low (Gu et al. 2013). | Bacteria |
Pseudomonadota | Mtr of E. coli (P0AAD2) |
2.A.42.1.3 | Low affinity (70 μM) tryptophan permease, coregulated with the enzyme tryptophanase. It functions in tryptohan degradation, yielding carbon and nitrogen (Gu et al. 2013). | Bacteria |
Pseudomonadota | TnaB of E. coli |
2.A.42.1.4 | Tyrosine permease (most similar in sequence to Mtr of E. coli) | Bacteria |
Pseudomonadota | TutB of Erwinia herbicola |
2.A.42.1.5 | Putative aromatic amino acid permease | Bacteria |
Pseudomonadota | Putative ArAA permease of Francisella tularensis |
2.A.42.1.6 | γ-aminobutyric acid (GABA):Na+ symporter (Zhao et al. 2012). The GABA Km is 40 µM, and uptake is inhibited by L-Asn and L-Gln. | Bacteria |
Actinomycetota | GabP of Corynebacterium glutamicum |
2.A.42.1.7 | Aromatic amino acid permease of 367 aas and 11 TMSs | Archaea |
Euryarchaeota | ArAAAP family member of Thermococcus barophilus |
2.A.42.1.8 | Uncharacterized amino acid uptake porter of 399 aas and 11 TMSs. | Bacteria |
Candidatus Wolfebacteria | UP of Candidatus Wolfebacteria bacterium |
2.A.42.2.1 | Serine permease | Bacteria |
Pseudomonadota | SdaC of E. coli (P0AAD6) |
2.A.42.2.2 | Threonine/Serine permease | Bacteria |
Pseudomonadota | TdcC of E. coli (P0AAD8) |
2.A.42.2.3 | Inner membrane transport protein, YhjV, of 423 aas and 11 TMSs. It may play a role in the transport of fluorophores (fluorescent dyes) (Salcedo-Sora et al. 2021) as well as melatonin (Yang et al. 2022). | Bacteria |
Pseudomonadota | YhjV of Escherichia coli |
2.A.42.2.4 | Inner membrane inducible, anaerobic, cysteine uptake transport protein, CyuP (DlsT; YhaO) of 443 aas and 11 TMSs (Loddeke et al. 2017). It is in a bicistronic operon with CyuA, an iron-sulfur-containing cysteine desulfidase, and this operon is regulated by the CyuR protein and induced maximally under anaerobic conditions. L-cysteine, D-cysteine, and a few other sulfur-containing compounds can serve as inducers. This system has been characterized both in E. coli and in S. enterica (Loddeke et al. 2017). | Bacteria |
Pseudomonadota | CyuP of Escherichia coli |
2.A.42.2.5 | Inner membrane transport protein YqeG | Bacteria |
Pseudomonadota | YqeG of Escherichia coli |