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sublancin family glycopeptide
This family represents sublancin, a small bacteriocin active against Gram-positive bacteria. This family appears to be restricted to Bacilli. Sublancin was thought to be a lantibiotic but was later shown to be an S-linked glycopeptide [1,2]. Glycosylation is essential for its antimicrobial activity. Sublancin is biosynthesised as a precursor peptide bearing an N-terminal leader peptide, and a C-terminal core peptide that is converted into the mature peptide [1]. Sublancin comprises two alpha helices and a well-defined inter-helical loop [3]. Sublancin inhibits B.cereus spore outgrowth, after the germination stage, approximately 1000-fold better than it inhibits exponential growth of the same cells and inhibits B.subtilis strain ATCC6633 and B. megaterium strain 14581 [2]. [1]. 21196935. Sublancin is not a lantibiotic but an S-linked glycopeptide. Oman TJ, Boettcher JM, Wang H, Okalibe XN, van der Donk WA;. Nat Chem Biol. 2011;7:78-80. [2]. 9722542. Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168. Paik SH, Chakicherla A, Hansen JN;. J Biol Chem. 1998;273:23134-23142. [3]. 24405370. NMR structure of the S-linked glycopeptide sublancin 168. Garcia De Gonzalo CV, Zhu L, Oman TJ, van der Donk WA;. ACS Chem Biol. 2014;9:796-801. (from Pfam)
Members of this family, including sublancin, are post-ribosomal natural products (PRNP) with an S-linked glycosylation. Sublancin itself also has two disulfide bonds. A related gene cluster in Bacillus cereus E33L includes the four Cys involved in the disulfide cluster but lacks the region with the glycosylated Cys. These score ~ 27 by this HMMER3 model and are excluded.
bacteriocin sublancin-168
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