General features of transmembrane beta barrels from a large database

Large datasets contribute new insights to subjects formerly investigated by exemplars. We used coevolution data to create a large, high-quality database of transmembrane (3 barrels (TMBB). By applying simple feature detection on generated evolutionary contact maps, our method (IsItABarrel) achieves 95.88% balanced accuracy when discriminating among protein classes. Moreover, comparison with IsItABarrel revealed a high rate of false positives in previous TMBB algorithms. In addition to being more accurate than previous datasets, our database (available online) contains 1,938,936 bacterial TMBB proteins from 38 phyla, respectively, 17 and 2.2 times larger than the previous sets TMBB- DB and OMPdb. We anticipate that due to its quality and size, the database will serve as a useful resource where high-quality TMBB sequence data are required. We found that TMBBs can be divided into 11 types, three of which have not been previously reported. We find tremendous variance in proteome percentage among TMBB-containing organisms with some using 6.79% of their proteome for TMBBs and others using as little as 0.27% of their proteome. The distribution of the lengths of the TMBBs is suggestive of previously hypothesized duplication events. In addition, we find that the C terminal (3 signal varies among different classes of bacteria though its consensus sequence is LGLGYRF. However, this (3 signal is only characteristic of prototypical TMBBs. The ten non-prototypical barrel types have other C-terminal motifs, and it remains to be determined if these alternative motifs facilitate TMBB insertion or perform any other signaling function.

Automated summary

By utilizing coevolution data, we have created a large and high-quality database of transmembrane proteins. Our method, IsItABarrel, achieves a balanced accuracy of 95.88% in discriminating among protein classes. Compared to previous algorithms, IsItABarrel shows a high rate of false positives. The database contains a significantly larger number of bacterial TMBB proteins compared to previous sets, and we anticipate it will serve as a valuable resource for researchers.