Part:BBa_K808005
tctB_197: small subunit B2 of the tripartite tricarboxylate transporter family
The small subunit B1 of the tripartite tricarboxylate transporter family (tctB_197, 20,44 kDa) was isolated from Comamonas testosteroni KF-1. The tripartite tricarboxylate transporter system consists of three different proteins: a periplasmatic solute binding receptor, a membrane protein with 12 putative transmembrane alpha-helical spanners (in this case tctB_197), and a small poorly conserved membrane proteine with four putative transmembrane alpha-helical spanners.[1] The strain was purchased from Leibniz Institute DMSZ-German Collection of Microorganism and Cell Cultures (DMSZ no. 14576). To characterized the structure of the tctB_197 bioinformatic tools like Protein Homology/anologY Recognition Engine V 2.0 (PHYRE2), I-TASSER servers, and TMHMM was used. The TMHMM predicted a transmembrane protein with 4 alpha-helical spanners (Fig. 1). The NCBI Protein BLAST results shows that the tctB_197 subunit B2 belongs to the tctB superfamily. Phyre2 an I-Tasser server homology modelling did not give a significant result for the structure of the tctB_197 subunit B2.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 18
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 522
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 345
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- Kamimura, N., T. Aoyama, et al. (2010). "Characterization of the protocatechuate 4,5-cleavage pathway operon in Comamonas sp. strain E6 and discovery of a novel pathway gene." Appl Environ Microbiol 76(24): 8093-8101.
- Winnen, B., R. N. Hvorup, et al. (2003). "The tripartite tricarboxylate transporter (TTT) family." Res Microbiol 154(7): 457-465.
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