HAAAP family


The Hydroxy/Aromatic Amino Acid Permease Family is a member of the large Amino Acid-Polyamine-OrganoCation Superfamily of secondary carriers. Members of the HAAAP family all function in amino acid uptake. Homologues are present in a large number of Gram-negative and Gram-positive bacteria, with at least one member classified from archaea .

Structure

Proteins of the HAAAP family possess 403-443 amino acyl residues and exhibit eleven putative or established transmembrane α-helical spanners. These proteins exhibit topological features common to the eukaryotic amino acid/auxin permease family. These proteins also exhibit limited sequence similarity with some of the AAAP family members. A phylogenetic relationship has been proposed between members of the HAAAP family and APC family since they exhibit limited sequence similarity with one another.
As of early 2016, there is no crystal structural data available for members of the HAAAP family in RCSB.

Members of the HAAAP Family

The HAAAP family includes three well-characterized aromatic amino acid:H+ symport permeases of E. coli: a high affinity tryptophan-specific permease, Mtr, a low affinity tryptophan permease, TnaB, and a tyrosine-specific permease, TyrP, as well as two well-characterized hydroxy amino acid permeases, the serine permease, SdaC, of E. coli, and the threonine permease, TdcC, of E. coli.
SdaC of E. coli is also called DcrA, and together with a periplasmic protein DcrB, has been reported to play a role in phage DNA uptake in conjunction with an outer membrane receptor of the OMR family. Thus, FhuA transports phage T5 DNA while BtuB transports phage C1 DNA. DcuB is a putative lipoprotein found only in enteric bacteria.
All members of the HAAAP family can be found in the .

Transport Reaction

The generalized transport reaction catalyzed by proteins of the HAAAP family is:
Amino acid + nH+ → Amino acid + nH+.