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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).

Accession Number:P13068
Protein Name:LANN aka SPAN aka NISA
Length:57
Molecular Weight:5963.00
Species:Lactococcus lactis (subsp [1360]
Location1 / Topology2 / Orientation3: Secreted1
Substrate molecule

Cross database links:

Pfam: PF02052   

Gene Ontology

GO:0005102 F:receptor binding
GO:0019835 P:cytolysis
GO:0050830 P:defense response to Gram-positive bacterium

References (10)

[1] “Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic.”  Buchman G.W.et.al.   3141403
[2] “Characterization of the nisin gene as part of a polycistronic operon in the chromosome of Lactococcus lactis ATCC 11454.”  Steen M.T.et.al.   1905517
[3] “Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product.”  Kaletta C.et.al.   2493449
[4] “Biosynthesis of the lantibiotic nisin: genomic organization and membrane localization of the NisB protein.”  Engelke G.et.al.   1482192
[5] “Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity.”  Kuipers O.P.et.al.   7689965
[6] “The structure of nisin.”  Gross E.et.al.   5131162
[7] “NMR studies of lantibiotics. The structure of nisin in aqueous solution.”  van de Ven F.J.et.al.   1765078
[8] “Solution structures of nisin A and its two major degradation products determined by NMR.”  Lian L.-Y.et.al.   1575686
[9] “NMR and circular dichroism studies of the lantibiotic nisin in non-aqueous environments.”  van den Hooven H.W.et.al.   8454055
[10] “15N- and 13C-labeled media from Anabaena sp. for universal isotopic labeling of bacteriocins: NMR resonance assignments of leucocin A from Leuconostoc gelidum and nisin A from Lactococcus lactis.”  Sailer M.et.al.   8418850

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FASTA formatted sequence 
1:	MSTKDFNLDL VSVSKKDSGA SPRITSISLC TPGCKTGALM GCNMKTATCH CSIHVSK