The
most interesting similarity found was to the structure of theHelicobacter pylori protein Tip-α (Tumor necrosis factor α
(TNF-α) inducing protein) (PDB IDs: 2WCQ, 3VNC) with an RMSD of 3.08 Å
over the length of 136 amino acids. Tip-α is an unusual virulence
factor, being able to penetrate gastric cells and stimulate the
production of the TNF- α and simultaneously activate the NF-κB pathway
[17], finally resulting in a strong carcinogenic effect. Tip-α is
highly expressed during bacterial infection [22] and forms
homodimers in its active state.
Finally, another pairwise alignment between the structure of calcium
dodecin (Rv0397) from Mycobacterium tuberculosis (PDB ID: 3ONR)
and the structure of FTT_1539 had an RMSD of 2.19 Å over the length of
137 amino acids. Calcium dodecin is also classified as a member of the
SHS2 clan and is involved in secretion and signaling of proteins that
help regulate the life cycle of bacteria [23]. The structural fold
of calcium dodecin allows it to form a pocket-like motif which binds
calcium and is similar to metal or flavin binding sites [23].