With advances in sequencing technology, uncharacterized proteins and domains of
unknown function (DUFs) are rapidly accumulating in sequence databases and offer an …

Abstract Microcin B17 (MccB17) is an antibacterial peptide produced by strains of
Escherichia coli harboring the plasmid-borne mccB17 operon. MccB17 possesses many …

In order to accelerate drug discovery, a simple, reliable, and cost-effective system for high-
throughput identification of a potential antibiotic mechanism of action is required. To facilitate …

Thiazole/oxazole-modified microcins (TOMMs) encompass a recently defined class of
ribosomally synthesized natural products with a diverse set of biological activities. Although …

YcaO enzymes catalyze ATP-dependent post-translation modifications on peptides,
including the installation of (ox/thi) azoline, thioamide and/or amidine moieties. Here we …

The introduction of azole heterocycles into a peptide backbone is the principal step in the
biosynthesis of numerous compounds with therapeutic potential. One of them is microcin …

Ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products
are of broad interest because of their intrinsic bioactivities and potential for synthetic biology …

TldD and TldE proteins are involved in the biosynthesis of microcin B17 (MccB17), an
Escherichia coli thiazole/oxazole-modified peptide toxin targeting DNA gyrase. Using a …

Escherichia coli microcin B (Ec-McB) is a posttranslationally modified antibacterial peptide
containing multiple oxazole and thiazole heterocycles and targeting the DNA gyrase. We …

Ribosomally synthesized posttranslationally modified peptides (RiPPs) are a rapidly
growing class of natural products with diverse structures and activities. In recent years, a …