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:
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.
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.
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.
Kazanov, M.D., A.G. Vitreschak, and M.S. Gelfand. (2007). Abundance and functional diversity of riboswitches in microbial communities. BMC Genomics 8: 347.
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.
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.
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.
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.
Sharma, R. and T.V. Mishanina. (2023). A riboswitch-controlled manganese exporter (Alx) tunes intracellular Mn concentration in at alkaline pH. bioRxiv.
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.
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]
Examples:
TC#	Name	Organismal Type	Example
2.A.109.1.1	*Tellurium resistance protein, TerC of 346 aas and 9 TMSs in a 5 + 4 TMS arrangement. Interactions with several other proteins including TerB have been demonstrated (Turkovicova et al.* 2016).**	Bacteria	*TerC of E. coli* (CAB42997)**

2.A.109.1.2	Alx protein of 323 aas and 9 TMSs in a 2 + 3 + 4 TMS arrangement.	Bacteria	*Alx of Neisseria meningitidis* (F0N2E7)**

2.A.109.1.3	YceF of 262 aas; possibly with 8 TMSs in a 2 + 2 + 2 + 2 TMS arrangement.	Bacteria	*YceF of Bacillus cereus* (B5UIP4)**

2.A.109.1.4	*Putative transporter, YkoY (with 324 aas and 9 TMSs in a 1 + 2 + 2 + 4 TMS arrangement) (Kazanov et al.* 2007; Meyer et al. 2011)**	Bacteria	YkoY of Bacillus subtilis (O34997)

2.A.109.1.5	TerC family efflux pump of 210 aas with 6 TMSs in a 3 + 3 TMS arrangement.	α-Proteobacteria	TerC family member of Sinorhizobium fredii

2.A.109.1.6	Uncharacterized protein of 352 aas with 8 TMSs in a 4 + 4 TMS arrangement.	Plants	*UP of Brachypodium distachyon* (Purple false brome) (Trachynia distachya)**

2.A.109.1.7	Membrane protein induced over 100x by alkaline conditions, Alx or YgjT of 321 aas and 9 TMSs (Stancik et al. 2002). This riboswitch-controlled manganese exporter (Alx) tunes intracellular Mn²⁺ concentration in E. coli at alkaline pH. A set of acidic residues in the predicted TMSs of Alx play a role in Mn²⁺ export (Sharma and Mishanina 2023).		YgjT or Alx of E. coli

Examples:
TC#	Name	Organismal Type	Example
2.A.109.2.1	TerC homologue of 286 aas with 8 TMSs in a 2 + 1 + 1 + 2 + 2 TMS arrangement.	Planctomycetes	TerC homologue of Rhodopirellula baltica

2.A.109.2.2	Hypothetical protein of 300 aas and 7 putative TMSs	Planctomycetes	HP of Rhodopirellula baltica

2.A.109.2.3	8 TMS membrane protein including a transmembrane domain homologous to other proteins in the TerC family (2.A.109) with the transmembrane domain having a 4 + 4 TMS arrangement, and a C-terminal domain (residues 622 - 889) with high sequence identity with hemolysin C and all members of the HlyC family (TC# 1.C.126), including some Mg²⁺ exporters in Cyclin M Mg²⁺ Exporter (CNNM) (TC family 1.A.112). The hydrophilic N-terminal CBS domain is an integrase domain but may bind ATP (Huang et al. 2021).	Proteobacteria	Membrane protein of E. coli

Examples:
TC#	Name	Organismal Type	Example
2.A.109.3.1	DUF475; PRK14013 protein (341 aas; 9 or 10 TMSs in a 1 or 2 + 1 + 1 + 2 + 2 + 2 TMS arrangement).	Archaea	*DUF475 protein of Methanocaldococcus vulcanius* (C9RH03)**

2.A.109.3.2	TerC homolog of 399 aas and 10 TMSs in a 2 + 1 + 1 + 2 + 2 + 2 TMS arrangement.		TerC of Gordonia aichiensis

Examples:
TC#	Name	Organismal Type	Example
Examples:
TC#	Name	Organismal Type	Example