Sequence analysis of a newly identified fms20 variant with predicted structure
We report the identification and sequence characterization of a novel Enterococcus faecium fms20 variant. The protein sequence encodes a large polypeptide with a predicted N-terminal signal peptide, multiple ß-sheet–rich domains, and a C-terminal transmembrane helix consistent with an isopeptide-forming domain-containing fimbrial protein. Using AlphaFold structure prediction, we observed several well-folded domains arranged in tandem, connected by flexible linkers. These features are characteristic of surface-associated adhesion or receptor proteins. The deposited sequence and predicted structure provide a resource for further functional and evolutionary studies of the fms20 gene family.