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Yatao Jiang "
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Bioinformatic Survey of S-Layer Proteins in Bifidobacteria
[PDF]
Juan Li, Yihao Shen, Yatao Jiang, Le He, Zhongke Sun
Computational Molecular Bioscience (CMB)
,
2018,
DOI: 10.4236/cmb.2018.82003
Bifidobacterium genus. Multiple
alignments suggest S-layer proteins are relatively conservative. Phylogenetic
analysis of 24 S-layer (domain) protein sequences groups them into three
distinct clusters, with the majority species in Cluster-2. S-layer (domain)
protein has a universe motif DUF4381, though its function is unknown.
Meanwhile, two other motifs CARDB and EphA2_TM involved in cell adhesion and
cell signaling respectively, presented in most S-layer (domain) protein in bifidobacteria.
All S-layer proteins have a typical N-terminal Sec-dependent signal peptide and
a C-terminal trans-membrane region. Homological modeling of representative
S-layer proteins from each cluster revealed a few unique structural features. All representative S-layer proteins have a plenty of β-meander motif that exclusively composed by β-barrel structural architectures linked together by hairpin loops.
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