| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
1.C.20.1.1 | Class I lantibiotic bacteriocin Nisin precursor (Nisin A; Nisin Z; Nisin F) (has a mersacidin-like Lipid II domain, and forms Lipid II-dependent pores) (Brötz et al., 1998). Its activity is enhanced by the SlpB surface layer protein (Q09FL7) of Lactobacillus crispatus (Sun et al. 2017). Bacteriocin SK2-659 was effective against pathogenic bacteria such as Helicobacter pylori. The bacteriocin produced by L. lactis SK2-659, identified as nisin Z, disrupts bacterial membranes via pore formation, leading to cell lysis. Metabolomic profiling further highlighted its ability to increase carbohydrate and amino acid metabolism, supporting cell growth and survival in acidic environments. Also, amino acid metabolism (elevated tryptophan, tyrosine, histidine) supports acid tolerance and immune modulation (Kingkaew et al. 2025). Nisin monomers dimerize by forming β-sheets in a POPE:POPG lipid bilayer and oligomerize further to form stable transmembrane channels. These nisin dimers use Lipid II as a dimer interface to incur enhanced stability (Kingkaew et al. 2025).An engineered nisin analogue with a hydrophobic moiety attached at position 17 selectively inhibits Enterococcus faecium strains (Guo et al. 2024). | Bacteria |
Bacillota | Nisin precursor of Lactococcus lactis |
|
1.C.20.1.2 | Class I lantibiotic bacteriocin Gallidermin precursor (has a mersacidin-like Lipid II domain, and forms Lipid II-dependent pores) (Sahl and Bierbaum, 1998). The genetic organization, biosynthesis, modification, excretion, extracellular activation of the modified pre-peptide by proteolytic processing, self-protection of the producer, gene regulation, structure, and mode of action have been reviewed (Götz et al. 2014). The Gallidermin-lipid II complex probably forms water pores in the membrane (Pokhrel et al. 2019). It complexes Lipid II more tightly than it forms transmembrane channels (Pokhrel et al. 2021). | Bacteria |
Bacillota | Gallidermin precursor of Staphylococcus gallinarum |
|
1.C.20.1.4 | Class I lantibiotic bacteriocin Mutacin BNY266 | Bacteria |
Bacillota | Mutacin of Streptococcus mutans |
|
1.C.20.1.5 | Class I lantibiotic bacteriocin, Subtilin precursor | Bacteria |
Bacillota | Subtilin of Bacillus subtilis |
|
1.C.20.1.6 | Class I lantibiotic bacteriocin, Epidermin precursor (has a mersacidin-like Lipid II domain, and forms Lipid II-dependent pores) (Sahl & Bierbaum, 2008). The genetic organization, biosynthesis, modification, excretion, extracellular activation of the modified pre-peptide by proteolytic processing, self-protection of the producer, gene regulation, structure, and mode of actionhave been reviewed (Götz et al. 2014). | Bacteria |
Bacillota | Epidermin of Staphylococcus epidermidis |
|
1.C.20.1.8 | Mutacin 1140 (MU1140) precursor (homologous to several lantibiotics (Smith et al., 2008)). MU1140-lipid II complexes form water permeating membrane pores (Pokhrel et al. 2019). A single chain of MU1140 complexed with lipid II allows transport across the membrane via a single-file water transport mechanism. The ordering of the water molecules in the single-file chain region as well as the diffusion behavior is similar to those observed in other biological water channels. Multiple complexes of MU1140-lipid II in the membrane showed enhanced permeability for the water molecules, as well as a noticeable membrane distortion and lipid relocation, suggesting that a higher concentration of MU1140 assembly in the membrane can cause significant disruption of the bacterial membrane (Pokhrel et al. 2019). It complexes Lipid II more tightly than it forms transmembrane channels (Pokhrel et al. 2021). | Bacteria |
Bacillota | Mutacin 1140 of Streptococcus mutans (O68586) |
|
1.C.20.2.1 | Class I lantibiotic bacteriocin, Pep5, of 60 aas (Suzuki et al. 2024). | Bacteria |
Bacillota | Pep5 lantibiotic of Staphylococcus epidermidis |
|
1.C.20.2.2 | Class I lantibiotic bacteriocin, Epilancin K7 precursor of 55 aas and 0 TMSs. It penetrates into the hydrophobic carbon region of the lipid bilayer upon the imposition of a delta psi and permeabilizes the bilayer (Driessen et al. 1995). | Bacteria |
Bacillota | Epilancin K7 of Staphylococcus epidermidis |
|
1.C.20.2.3 | Epilancin 10025 of 55 aas and 0 TMSs. | Bacteria |
Bacillati, Bacillota | Epilancin 10025 of Staphylococcus epidermidia |