The TerC family (Pfam 03741) includes the E. coli TerC protein (TC# 2.A.109.1.1) which has been implicated in tellurium resistance.[2] It is hypothesized to catalyze efflux of tellurium ions.[2][3] 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.[2]
A homologue in Arabidopsis thaliana (TC# 9.A.30.2.1) may function in prothylakoid membrane biogenises during early chloroplast development.[4] 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.[5] It may be part of a metal sensing stress response system.[6] The co-presence of TerC and TerE but not TerF correlates with tellurite resistance when several hundred bacterial strains were assayed.[7]
^ abcBurian, J.; Tu, N.; Kl'ucár, L.; Guller, L.; Lloyd-Jones, G.; Stuchlík, S.; Fejdi, P.; Siekel, P.; Turna, J. (1998-01-01). "In vivo and in vitro cloning and phenotype characterization of tellurite resistance determinant conferred by plasmid pTE53 of a clinical isolate of Escherichia coli". Folia Microbiologica. 43 (6): 589–599. doi:10.1007/bf02816374. ISSN0015-5632. PMID10069007. S2CID44237747.
^Kormutakova, R.; Klucar, L.; Turna, J. (2000-06-01). "DNA sequence analysis of the tellurite-resistance determinant from clinical strain of Escherichia coli and identification of essential genes". BioMetals. 13 (2): 135–139. doi:10.1023/A:1009272122989. ISSN0966-0844. PMID11016400. S2CID22672098.