Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain
This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.
Feature 1: metal binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:H H [QEN] [QH]
Evidence:
Structure:3H9A: Bacillus subtilis bacilysin biosynthesis protein BacB binds cobalt; contacts at 4.0A
Comment:The four-coordinate metallocenter usually includes three histidines and one glutamate; however, proteins in this subfamily may bind metal via different amino acids.
Jiyao W et al.(2023). "The conserved domain database in 2023.",