HMM Summary Page: TIGR02595

FunctionPEP-CTERM protein-sorting domain
Trusted Cutoff16.00
Domain Trusted Cutoff16.00
Noise Cutoff9.55
Domain Noise Cutoff9.55
Isology Typedomain
HMM Length24
Mainrole CategoryCell envelope
Subrole CategorySurface structures
AuthorHaft DH, Selengut J
Entry DateJun 6 2005 2:46PM
Last ModifiedJul 16 2012 5:51PM
CommentThis model describes a 25-residue domain that includes a near-invariant Pro-Glu-Pro (PEP) motif, a thirteen residue strongly hydrophobic sequence likely to span the membrane, and a five-residue strongly basic motif that often contains four Arg residues. In nearly every case, this motif is found within nine residues, and usually within five residues, of the extreme C-terminus of the protein. Proteins with this motif typically have signal sequences at the N-terminus. This region appears many times per genome or not at all, and co-occurs in genomes with a proposed protein-sorting integral membrane protein we designate exosortase (see TIGR02602). PEP-CTERM proteins frequently are poorly conserved, Ser/Thr-rich proteins and may become extensively modified proteinaceous constituents of extracellular material in bacterial biofilms.
ReferencesDR PFAM; PF07589; Protein of unknown function (DUF1555) RN [1] RM 16930487 RA Haft DH, Paulsen IT, Ward N, Selengut JD RT Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic. RL BMC Biol. 2006 Aug 24;4(1):29
Genome PropertyGenProp0326: protein sorting system, PEP-CTERM/exosortase (generic) (HMM)