Tellurium ion resistance explained

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.[1]

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.[2] It is hypothesized to catalyze efflux of tellurium ions.[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.

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]

Function

The reaction proposed to be catalyzed by TerC is:

tellurium ions (in) → tellurium ions (out).

See also

Further reading

Notes and References

  1. Web site: 2.A.109 The Tellurium Ion Resistance (TerC) Family. Transporter Classification Database. 2016-02-26.
  2. Burian. 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. 0015-5632. 10069007. 10.1007/bf02816374. 44237747.
  3. 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. 10.1023/A:1009272122989. 0966-0844. 11016400. 22672098.
  4. Kwon. Kwang-Chul. Cho. Myeon Haeng. 2008-08-01. Deletion of the chloroplast-localized AtTerC gene product in Arabidopsis thaliana leads to loss of the thylakoid membrane and to seedling lethality. The Plant Journal. 55. 3. 428–442. 10.1111/j.1365-313X.2008.03523.x. 1365-313X. 18429937. free.
  5. Turkovicova. L.. Smidak. R.. Jung. G.. Turna. J.. Lubec. G.. Aradska. J.. 2016-01-09. Proteomic analysis of the TerC interactome: Novel links to tellurite resistance and pathogenicity. Journal of Proteomics. 10.1016/j.jprot.2016.01.003. 1876-7737. 26778143. 136. 167–73.
  6. Anantharaman. Vivek. Iyer. Lakshminarayan M.. Aravind. L.. 2012-10-30. Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing. Molecular BioSystems. 8. 12. 3142–3165. 10.1039/c2mb25239b. 1742-2051. 4104200. 23044854.
  7. Orth. Dorothea. Grif. Katharina. Dierich. Manfred P.. Würzner. Reinhard. 2007-03-01. Variability in tellurite resistance and the ter gene cluster among Shiga toxin-producing Escherichia coli isolated from humans, animals and food. Research in Microbiology. 158. 2. 105–111. 10.1016/j.resmic.2006.10.007. 0923-2508. 17317110. free.

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