HMM Summary Page: TIGR03793

FunctionNHLP leader peptide domain
Trusted Cutoff50.90
Domain Trusted Cutoff50.90
Noise Cutoff43.40
Domain Noise Cutoff43.40
Isology Typedomain
HMM Length77
AuthorHaft DH
Entry DateJul 16 2009 2:57PM
Last ModifiedMar 10 2014 5:46PM
CommentThis HMM represents a domain that is conserved among a large number of putative ribosomal natural products (RNP) precursor, including the thiazole/oxazole-modified microcins (TOMMs). As a leader peptide domain, likely to be removed from the mature product, this domain is unusual in several ways. First, it is longer than most previously described RNP leader peptides. Second, most of the domain is homologous to nitrile hydratase alpha subunits. Finally, it appears that this domain correlates with a specific family of cleavage/export proteins while members undergo modifications by different classes of peptide maturase, including cyclodehydratases, lantibiotic synthases, radical SAM peptide maturases. This family is expanded especially in Pelotomaculum thermopropionicum SI.
ReferencesRN [1] RM PMID:20500830 RT Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family. RA Haft DH, Basu MK, Mitchell DA RL BMC Biol. 2010 May 25;8:70. RN [2] RM PMID:22983711 RT Metagenome mining reveals polytheonamides as posttranslationally modified ribosomal peptides. RA Freeman MF, Gurgui C, Helf MJ, Morinaka BI, Uria AR, Oldham NJ, Sahl HG, Matsunaga S, Piel J RL Science. 2012 Oct 19;338(6105):387-90. doi: 10.1126/science.1226121.
Genome PropertyGenProp0807: bacteriocin system, heterocycle biosynthesis group (HMM)
GenProp0861: bacteriocin system, NHLP (nif11/nitrile hydratase leader peptide) transport group (HMM)