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competence type IV pilus minor pilin ComGF
ComGF is a family of putative bacterial competence proteins. [1]. 9723928. Cell surface localization and processing of the ComG proteins, required for DNA binding during transformation of Bacillus subtilis. Chung YS, Breidt F, Dubnau D;. Mol Microbiol. 1998;29:905-913. (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)
ComGF is one of several minor pilins in the type IV pilus involved in the competence system of natural transformation by various Gram-positive bacteria. Oddly, while nearly all members have an N-terminal region with a consensus site for cleavage and methylation, ComGF from Bacillus subtilis appears N-terminally truncated, and may be functional despite the truncation.
ComGF family competence protein
ComGF family competence protein similar to Bacillus licheniformis late competence protein ComGF
This model describes many but not all examples of the N-terminal region of bacterial proteins that resemble type IV pilins at their N-terminus, with a cleavage site G^FxxxE followed by a hydrophobic stretch. The new N-terminal residue, usually Phe, is methylated. Separate domains of the prepilin peptidase appear responsible for cleavage and methylation. Proteins with this N-terminal region include type IV pilins and other components of pilus biogenesis, competence proteins, and type II secretion proteins. Typically several proteins in a single operon have this N-terminal domain. The N-terminal cleavage and methylation site is described by PROSITE motif PS00409 as [KRHEQSTAG]-G-[FYLIVM]-[ST]-[LT]-[LIVP]-E-[LIVMFWSTAG](14).
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