| Accession | TIGR03370 |
| Name | VPLPA-CTERM |
| Function | VPLPA-CTERM protein sorting domain |
| Trusted Cutoff | 25.35 |
| Domain Trusted Cutoff | 25.35 |
| Noise Cutoff | 17.60 |
| Domain Noise Cutoff | 17.60 |
| Isology Type | subfamily_domain |
| HMM Length | 25 |
| Author | Haft DH |
| Entry Date | Mar 23 2007 3:05PM |
| Last Modified | Feb 10 2012 12:30PM |
| Comment | A probable protein export sorting signal, PEP-CTERM, was described by Haft, et al. (PMID:16930487). It is predicted to interact with a putative transpeptidase we designate exosortase. This model describes a variant with conserved motif VPLPA, rather than VPEP. It appears to be the recognition sequences for exosortase D (TIGR04152). This variant is found prominently in two members of the Rhodobacterales, namely Jannaschia sp. CCS1 and Roseobacter denitrificans OCh 114. One interesting member protein has a full-length duplication and therefore two copies of this putative sorting domain. |
| References | RN [1]
RM PMID:22037399
RT Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification.
RA Haft DH, Payne SH, Selengut JD
RL J Bacteriol. 2012 Jan;194(1):36-48. Epub 2011 Oct 28.
RN [2]
RM PMID: 16930487
RT Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic.
RA Haft DH, Paulsen IT, Ward N, Selengut JD
RL BMC Biol. 2006 Aug 24;4:29. |
| Genome Property | GenProp0986: protein sorting system, VPLPA-CTERM/exosortase D (HMM) |
