TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*2.A.42.1.1









Tyrosine permease
Bacteria
Proteobacteria
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
Proteobacteria
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
Proteobacteria
TnaB of E. coli
*2.A.42.1.4









Tyrosine permease (most similar in sequence to Mtr of E. coli)
Bacteria
Proteobacteria
TutB of Erwinia herbicola
*2.A.42.1.5









Putative aromatic amino acid permease

Bacteria
Proteobacteria
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
Actinobacteria
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
Proteobacteria
SdaC of E. coli (P0AAD6)
*2.A.42.2.2









Threonine/Serine permease
Bacteria
Proteobacteria
TdcC of E. coli (P0AAD8)
*2.A.42.2.3









Inner membrane transport protein YhjV
Bacteria
Proteobacteria
YhjV of Escherichia coli
*2.A.42.2.4









Inner membrane inducible, anaerobic, cysteine uptake transport protein, CyuP (YhaO) of 434 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
Proteobacteria
CyuP of Escherichia coli
*2.A.42.2.5









Inner membrane transport protein YqeG
Bacteria
Proteobacteria
YqeG of Escherichia coli