Difference between revisions of "Part:BBa K808002"

 
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<partinfo>BBa_K808002 short</partinfo>
 
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tctA_503: large subunit A1 of the tripartite tricarboxylate transporter family  
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The large subunit A1 of the tripartite tricarboxylate transporter family (tctA_503, 52,98 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 tctA_503), and a small poorly conserved membrane proteine with four putative transmembrane alpha-helical spanner<sup>[1]</sup>..The strain was purchased from Leibniz Institute DMSZ-German Collection of Microorganism and Cell Cultures (DMSZ no. 14576). The original sequence contains a Pst1 recognition site. To eliminate this recognition site a directed-site mutagenic PCR was performed. (For more datails: link zu dem PCR protokoll und dem Labjournal, wo isolations PCR  beschrieben wird) To characterized the structure of the tctA_503 bioinformatic tools like '''P'''rotein '''H'''omology/anolog'''Y''' '''R'''ecognition '''E'''ngine V 2.0 (PHYRE2), I-TASSER  servers, and TMHMM was used. The TMHMM predicted a  transmembrane protein with 11 alpha-helical spanners (Fig. 1). The N-teminus is with a probability of 98 %  in cytoplasmatic.
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The NCBI Protein BLAST results shows that the tctA_503 subunit A1 belongs to the tctA superfamily. PHYRE2 and I-Tasser server homology modelling did not give a significant result for the structure of the tctA_503 subunit A1.
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[[Image:File-tcta503_tmhmm.png|900px|thumb|center|Figure 1. '''TMHMM prediction of the tctA_503 subunit A1.''' It shows 11 alpha-helical spanners.]]
  
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K808002 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K808002 SequenceAndFeatures</partinfo>
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==References==
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[1] Sasoh, M., E. Masai, et al. (2006). "Characterization of the terephthalate degradation genes of Comamonas sp. strain E6." Appl Environ Microbiol 72(3): 1825-1832.
  
  

Revision as of 17:13, 23 September 2012

tctA_503: large subunit A1 of the tripartite tricarboxylate transporter family

The large subunit A1 of the tripartite tricarboxylate transporter family (tctA_503, 52,98 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 tctA_503), and a small poorly conserved membrane proteine with four putative transmembrane alpha-helical spanner[1]..The strain was purchased from Leibniz Institute DMSZ-German Collection of Microorganism and Cell Cultures (DMSZ no. 14576). The original sequence contains a Pst1 recognition site. To eliminate this recognition site a directed-site mutagenic PCR was performed. (For more datails: link zu dem PCR protokoll und dem Labjournal, wo isolations PCR beschrieben wird) To characterized the structure of the tctA_503 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 11 alpha-helical spanners (Fig. 1). The N-teminus is with a probability of 98 % in cytoplasmatic. The NCBI Protein BLAST results shows that the tctA_503 subunit A1 belongs to the tctA superfamily. PHYRE2 and I-Tasser server homology modelling did not give a significant result for the structure of the tctA_503 subunit A1.

Figure 1. TMHMM prediction of the tctA_503 subunit A1. It shows 11 alpha-helical spanners.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 1467
    Illegal AgeI site found at 712
  • 1000
    COMPATIBLE WITH RFC[1000]


References

[1] Sasoh, M., E. Masai, et al. (2006). "Characterization of the terephthalate degradation genes of Comamonas sp. strain E6." Appl Environ Microbiol 72(3): 1825-1832.