The Tellurium Ion Resistance (TerC) Family (TC# 2.A.109) is part of the Lysine Exporter (LysE) Superfamily. A representative list of proteins belonging to the TerC family can be found in the Transporter Classification Database.
Contents
TerC
The TerC family (Pfam 03741) includes the E. coli TerC protein (TC# 2.A.109.1.1) which has been implicated in tellurium resistance. It is hypothesized to catalyze efflux of tellurium ions. TerC is encoded by plasmid pTE53 from a clinical isolate of E. coli. It has 346 amino acyl residues (aas) and 9 putative transmembrane segments (TMSs) with a large hydrophilic loop between TMSs 5 and 6.
A homologue in Arabidopsis thaliana (TC# 9.A.30.2.1) may function in prothylakoid membrane biogenises during early chloroplast development. It has 384 aas and 7-8 putative TMSs. In E. coli, TerC forms a membrane complex with TerB as well as DctA, PspA, HslU, and RplK. The TerB/TerC complex may link different functional modules with biochemical activities of C4-dicarboxylate transport, inner membrane stress response (phage shock protein regulatory complex), ATPase/chaperone activity, and proteosynthesis. It may be part of a metal sensing stress response system. The co-presence of TerC and TerE but not TerF correlates with tellurite resistance when several hundred bacterial strains were assayed.
Function
The reaction proposed to be catalyzed by TerC is:
tellurium ions (in) → tellurium ions (out).