General Information
-
DRAMP ID
- DRAMP00036
-
Peptide Name
- Nisin A (Bacteriocin; Preclinical)
-
Source
- Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria)
-
Family
- Belongs to the type A lantibiotic family (Class I bacteriocin)
-
Gene
- spaN
-
Sequence
- ITSISLCTPGCKTGALMGCNMKTATCHCSIHVSK
-
Sequence Length
- 34
-
UniProt Entry
- P13068
-
Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+
-
Target Organism
-
- Gram-positive bacteria: Enterococcus, Lactobacillus, Lactococcus, Leuconostoc, Listeria, clostridium.
-
Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
-
Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
-
Binding Target
- Lipid II
Structure Information
-
Linear/Cyclic
- Cyclic
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four β-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28).
-
Stereochemistry
- L
-
Structure
- Non helix or strand structure
-
Structure Description
- Not found
-
Helical Wheel Diagram
-
PDB ID
- None
-
Predicted Structure
- There is no predicted structure for DRAMP00036.
Physicochemical Information
-
Formula
- C143H246N42O45S7
Absent Amino Acids
- DEFQRWY
Common Amino Acids
- CT
Mass
- 3498.2
PI
- 8.78
Basic Residues
- 5
Acidic Residues
- 0
Hydrophobic Residues
- 8
Net Charge
- +5
-
Boman Index
- -12.88
Hydrophobicity
- 0.415
Aliphatic Index
- 71.76
Half Life
-
- Mammalian:20 hour
- Yeast:30 min
- E.coli:>10 hour
Extinction Coefficient Cystines
- 250
Absorbance 280nm
- 7.58
Polar Residues
- 18
DRAMP00036
Comments Information
Function
- Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
PTM
- There are two dehydroalanines (S5; S33), one dehydrobutyrine (T2), which form one lanthionine (S3-C7) and four Beta-methyllanthionines (T8-C11; T13-C19; T23-C26; T25-C28).
Medical use
- Urogenital tract infections and spermicidal activity in-vivo; animal model
Literature Information
- ·Literature 1
-
Title
- Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic.
-
Pubmed ID
- 3141403
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Reference
- J Biol Chem. 1988 Nov 5;263(31):16260-16266.
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Author
- Buchman GW, Banerjee S, Hansen JN.
- ·Literature 2
-
Title
- The structure of nisin.
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Pubmed ID
- 5131162
-
Reference
- J Am Chem Soc. 1971 Sep 8;93(18):4634-4635.
-
Author
- Gross E, Morell JL.
- ·Literature 3
-
Title
- Solution structures of nisin A and its two major degradation products determined by n.m.r.
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Pubmed ID
- 1575686
-
Reference
- Biochem J. 1992 Apr 15;283 (Pt 2):413-420.
-
Author
- Lian LY, Chan WC, Morley SD, Roberts GC, Bycroft BW, Jackson D.