HMM Summary Page: TIGR03892

Functionthiazolylpeptide-type bacteriocin precursor
Trusted Cutoff25.00
Domain Trusted Cutoff25.00
Noise Cutoff21.35
Domain Noise Cutoff20.75
Isology Typesubfamily
HMM Length44
AuthorHaft DH
Entry DateDec 1 2009 12:16AM
Last ModifiedMar 14 2011 12:39PM
CommentMembers of this protein family are the precursors of a family of small bacteriocins (i.e. microcins) with thiopeptide type modifications, a highly modified subclass of heterocycle-containing peptide antibiotics. Members tend to be found clustered in genomes with proteins recognized by TIGR03891 and proteins/domains annotated as lantibiotic dehydratase (PF04737, PF04738), and with a cyclodehydratase/docking protein fusion protein characteristic of heterocycle formation. The seed alignment includes both an N-terminal leader peptide region and a C-terminal low-complexity region consisting mostly of Cys and Ser residues. Members with known function block translation by inhibiting translation factor activity.
ReferencesRN [1] RM PMID:19196969 RT Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin. RA Wieland Brown LC, Acker MG, Clardy J, Walsh CT, Fischbach MA RL Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2549-53. RN [2] RM PMID:19246004 RT Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications. RA Liao R, Duan L, Lei C, Pan H, Ding Y, Zhang Q, Chen D, Shen B, Yu Y, Liu W RL Chem Biol. 2009 Feb 27;16(2):141-7. RN [3] RM PMID:19265401 RT Thiostrepton biosynthesis: prototype for a new family of bacteriocins. RA Kelly WL, Pan L, Li C RL J Am Chem Soc. 2009 Apr 1;131(12):4327-34. RN [4] RM PMID:18406324 RT Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin. RA Harms JM, Wilson DN, Schluenzen F, Connell SR, Stachelhaus T, Zaborowska Z, Spahn CM, Fucini P RL Mol Cell. 2008 Apr 11;30(1):26-38.
Genome PropertyGenProp0807: bacteriocin system, heterocycle biosynthesis group (HMM)