| Accession | TIGR02595 |
| Name | PEP_exosort |
| Function | PEP-CTERM protein-sorting domain |
| Trusted Cutoff | 16.00 |
| Domain Trusted Cutoff | 16.00 |
| Noise Cutoff | 9.55 |
| Domain Noise Cutoff | 9.55 |
| Isology Type | domain |
| HMM Length | 24 |
| Mainrole Category | Cell envelope |
| Subrole Category | Surface structures |
| Author | Haft DH, Selengut J |
| Entry Date | Jun 6 2005 2:46PM |
| Last Modified | Jul 16 2012 5:51PM |
| Comment | This 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. |
| References | DR 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 Property | GenProp0326: protein sorting system, PEP-CTERM/exosortase (generic) (HMM) |
