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Type IV pilin Tt1218
The founding member of this family is Tt1218 that is a type IV pilin. This protein is likely involved in the formation of polymers that extend from the surface of the bacterial cell and could mediate a wide variety of functions such as adhesion, motility and natural competence. This domain is closely related to type II secretion pseudopilin EpsI. It consists of the canonical type IV pilin structural core comprising an alpha-helix packed against a four-stranded antiparallel beta-sheet [1]. Paper describing PDB structure 5g25. [1]. 27612581. Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins. Karuppiah V, Thistlethwaite A, Derrick JP;. J Struct Biol. 2016;196:375-384. (from Pfam)
prepilin-type N-terminal cleavage/methylation domain-containing protein
This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N-terminus of pilins and other proteins involved in secretion, see Pfam:PF00114, Pfam:PF05946, Pfam:PF02501 and Pfam:PF07596. (from Pfam)
type IV pilus modification protein PilV
Pilus systems categorized as type IV pilins differ greatly from one another, with some showing greater similarty to type II or type III secretion systems than to each other. Members of this protein family represent the PilV protein of type IV pilus systems as found in Pseudomonas aeruginosa PAO1, Pseudomonas syringae DC3000, Neisseria meningitidis MC58, Xylella fastidiosa 9a5c, etc.
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