BATMAS30: Amino acid substitution matrix for alignment of bacterial transporters

Roman A. Sutormin, Aleksandra B. Rakhmaninova, Mikhail S. Gelfand

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


Aligned amino acid sequences of three functionally independent samples of transmembrane (TM) transport proteins have been analyzed. The concept of TM-kernel is proposed as the most probable transmembrane region of a sequence. The average amino acid composition of TM-kernels differs from the published amino acid composition of transmembrane segments. TM-kernels contain more alanines, glycines, and less polar, charged, and aromatic residues in contrast to non-TM-proteins. There are also differences between TM-kernels of bacterial and eukaryotic proteins. We have constructed amino acid substitution matrices for bacterial TM-kernels, named the BATMAS (BActerial Transmembrane MAtrix of Substitutions) series. In TM-kernels, polar and charged residues, as well as proline and tyrosine, are highly conserved, whereas there are more substitutions within the group of hydrophobic residues, in contrast to non-TM-proteins that have fewer, relatively more conserved, hydrophobic residues. These results demonstrate that alignment of transmembrane proteins should be based on at least two amino acid substitution matrices, one for loops (e.g., the BLOSUM series) and one for TM-segments (the BATMAS series), and the choice of the TM-matrix should be different for eukaryotic and bacterial proteins.

Original languageEnglish
Pages (from-to)85-95
Number of pages11
JournalProteins: Structure, Function and Genetics
Issue number1
Publication statusPublished - 1 Apr 2003
Externally publishedYes


  • Amino acid substitution matrix
  • Comparative analysis
  • Evolution
  • Transmembrane segments
  • Transport proteins


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