HMM Summary Page: TIGR03370

FunctionVPLPA-CTERM protein sorting domain
Trusted Cutoff25.35
Domain Trusted Cutoff25.35
Noise Cutoff17.60
Domain Noise Cutoff17.60
Isology Typesubfamily_domain
HMM Length25
AuthorHaft DH
Entry DateMar 23 2007 3:05PM
Last ModifiedFeb 10 2012 12:30PM
CommentA 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.
ReferencesRN [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 PropertyGenProp0986: protein sorting system, VPLPA-CTERM/exosortase D (HMM)