TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.20.1.1









Class I lantibiotic bacteriocin Nisin precursor (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).

Bacteria
Firmicutes
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).

Bacteria
Firmicutes
Gallidermin precursor of Staphylococcus gallinarum
*1.C.20.1.3









Class I lantibiotic bacteriocin, Pep5
Bacteria
Firmicutes
Pep5 lantibiotic of Staphylococcus epidermidis
*1.C.20.1.4









Class I lantibiotic bacteriocin Mutacin BNY266
Bacteria
Firmicutes
Mutacin of Streptococcus mutans
*1.C.20.1.5









Class I lantibiotic bacteriocin, Subtilin precursor
Bacteria
Firmicutes
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
Firmicutes
Epidermin of Staphylococcus epidermidis
*1.C.20.1.7









Class I lantibiotic bacteriocin, Epilancin K7 precursor
Bacteria
Firmicutes
Epilancin K7 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).

Bacteria
Firmicutes
Mutacin 1140 of Streptococcus mutans (O68586)