HMM Summary Page: TIGR02532

Functionprepilin-type N-terminal cleavage/methylation domain
Trusted Cutoff16.30
Domain Trusted Cutoff16.30
Noise Cutoff16.30
Domain Noise Cutoff16.30
Isology Typedomain
HMM Length24
Mainrole CategoryCell envelope
Subrole CategorySurface structures
AuthorHaft DH
Entry DateMar 17 2005 4:26PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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).
ReferencesDR PROSITE; PDOC00342; PS00409; prokaryotic N-terminal methylation site DR PFAM; PF07963; prokaryotic N-terminal methylation motif DR HAMAP; MF_00221; 1 of 82
Genome PropertyGenProp0295: prokaryotic N-terminal cleavage/methylation, type IV pilin-like (HMM)