The Hydroxy/Aromatic Amino Acid Permease (HAAAP) Family (TC# 2.A.42) is a member of the large Amino Acid-Polyamine-OrganoCation (APC) Superfamily of secondary carrier proteins. Members of the HAAAP family all function in amino acid uptake. Homologues are present in many Gram-negative and Gram-positive bacteria, with at least one member classified from archaea (TC# 2.A.42.1.7, Thermococcus barophilus).
Proteins of the HAAAP family possess 403-443 amino acyl residues and exhibit eleven putative or established TransMembrane α-helical Spanners (TMSs). These proteins exhibit topological features common to the eukaryotic amino acid/auxin permease (AAAP) family (TC# 2.A.18). These proteins also exhibit limited sequence similarity with some of the AAAP family members. A phylogenetic relationship has been proposed between members of the HAP family and the APC family since they exhibit limited sequence similarity with one another.
As of early 2016, no crystal structural data is available for members of the HAAAP family in RCSB.
The HAAAP family includes three well-characterized aromatic amino acid/H+ symport permeases of E. coli and two hydroxy amino acid permeases. The aromatic amino acid/H+ symport permeases are:
The two hydroxy amino acid permeases are:
Thus, FhuA (TC# 1.B.14.1.4) transports phage T5 DNA while BtuB (TC# 1.B.14.3.1) transports phage C1 DNA (Samsonov et al., 2002). DcuB is a putative lipoprotein found only in enteric bacteria.
All members of the HAAAP family can be found in the Transporter Classification Database.
The generalized transport reaction catalyzed by proteins of the HAAAP family is:
Amino acid (out) + nH+ (out) → Amino acid (in) + nH+ (in).