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2.A.109 The Tellurium Ion Resistance (TerC) Family

The TerC family (Pfam 03741) includes the E. coli TerC protein which has been implicated in tellurium resistance (Burian et al. 1998). It is hypothesized to catalyze efflux of tellurium ions (Burian et al., 1998; Kormutakova et al. 2000). TerC is encoded by plasmid pTE53 from a clinical isolate of E. coli (Burian et al., 1998). It has 346 aas and 9 putative 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 (Kwon and Cho 2008). 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 (Turkovicova et al. 2016). It may be part of a metal sensing stress response system (Anantharaman et al. 2012). The co-presence of TerC and TerE but not TerF correlates with tellurite resistance when several hundred bacterial strains were assayed (Orth et al. 2007). Some of these proteins have C-terminal CBS domains.

The reaction proposed to be catalyzed by TerC is:

Tellurium ions (in) → tellurium ions (out)

References associated with 2.A.109 family:

Anantharaman, V., L.M. Iyer, and L. Aravind. (2012). Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing. Mol Biosyst 8: 3142-3165. 23044854
Burian, J., N. Tu, L. Kl'ucár, L. Guller, G. Lloyd-Jones, S. Stuchlík, P. Fejdi, P. Siekel, and J. Turna. (1998). 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 Microbiol (Praha) 43: 589-599. 10069007
Huang, Y., K. Mu, X. Teng, Y. Zhao, Y. Funato, H. Miki, W. Zhu, Z. Xu, and M. Hattori. (2021). Identification and mechanistic analysis of an inhibitor of the CorC Mg transporter. iScience 24: 102370. 33912817
Kazanov, M.D., A.G. Vitreschak, and M.S. Gelfand. (2007). Abundance and functional diversity of riboswitches in microbial communities. BMC Genomics 8: 347. 17908319
Kormutakova, R., L. Klucar, and J. Turna. (2000). DNA sequence analysis of the tellurite-resistance determinant from clinical strain of Escherichia coli and identification of essential genes. Biometals 13: 135-139. 11016400
Kwon, K.C. and M.H. Cho. (2008). Deletion of the chloroplast-localized AtTerC gene product in Arabidopsis thaliana leads to loss of the thylakoid membrane and to seedling lethality. Plant J. 55: 428-442. 18429937
Meyer, M.M., M.C. Hammond, Y. Salinas, A. Roth, N. Sudarsan, and R.R. Breaker. (2011). Challenges of ligand identification for riboswitch candidates. RNA Biol 8: 5-10. 21317561
Orth, D., K. Grif, M.P. Dierich, and R. Würzner. (2007). Variability in tellurite resistance and the ter gene cluster among Shiga toxin-producing Escherichia coli isolated from humans, animals and food. Res. Microbiol. 158: 105-111. 17317110
Sharma, R. and T.V. Mishanina. (2023). A riboswitch-controlled manganese exporter (Alx) tunes intracellular Mn concentration in at alkaline pH. bioRxiv. 37214827
Stancik, L.M., D.M. Stancik, B. Schmidt, D.M. Barnhart, Y.N. Yoncheva, and J.L. Slonczewski. (2002). pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli. J. Bacteriol. 184: 4246-4258. 12107143
Turkovicova, L., R. Smidak, G. Jung, J. Turna, G. Lubec, and J. Aradska. (2016). Proteomic analysis of the TerC interactome: Novel links to tellurite resistance and pathogenicity. J Proteomics. [Epub: Ahead of Print] 26778143