HMM Summary Page: TIGR03694
| Accession | TIGR03694 |
| Name | exosort_acyl |
| Function | N-acyl amino acid synthase, PEP-CTERM/exosortase system-associated |
| Trusted Cutoff | 111.95 |
| Domain Trusted Cutoff | 111.95 |
| Noise Cutoff | 52.80 |
| Domain Noise Cutoff | 52.80 |
| Isology Type | subfamily |
| EC Number | 2.3.1.- |
| HMM Length | 241 |
| Author | Haft DH |
| Entry Date | Nov 11 2008 10:03AM |
| Last Modified | Feb 22 2012 2:05PM |
| Comment | Members of this protein family are restricted to bacterial species with the PEP-CTERM/exosortase system predicted to act in exopolysaccharide-associated protein targeting. PSI-BLAST and CDD reveal relationships to the acyltransferase family that includes N-acyl-L-homoserine lactone synthetase, and recent work shows long-chain N-acyl amino acid biosynthesis activity. Several members of this family may be found in a single genome. These acyltransferases may produce a quorum signalling molecule or may contribute to chemical modifications in exopolysaccharide and biofilm structural material production. |
| References | RN [1] RM PMID:21840974 RT Long-chain N-acyl amino acid synthases are linked to the putative PEP-CTERM/exosortase protein-sorting system in Gram-negative bacteria. RA Craig JW, Cherry MA, Brady SF RL J Bacteriol. 2011 Oct;193(20):5707-15. Epub 2011 Aug 12. 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. |