View bacteriocin : nisin U Bookmark and Share

Accession BAC147
Name nisin U
Related Entries nisin-Anisin-ZNisin QNisin F
Gene nsuA
Class Lantibiotic
Producer Organism Lactococcus uberis ATCC 27958 [Gram-positive]
Taxonomy BacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus
Target organisms Active against Streptococcus pyogenes (10/11) - Streptococcus uberis (20/26) - Streptococcus agalactiae (2/4) - Streptococcus dysgalactiae (3/4) - Staphylococcus simulans (1/1) - Staphylococcus cohnii (1/1) - Lactococcus lactis (1/3) - Lactobacillus acidophilus (1/1) - Streptococcus mitis (2/2) -

NOTE: not active against Lactobacillus casei (0/1) - Streptococcus rattus (0/2) - Enterococcus faecalis (0/3) - Staphylococcus aureus (0/2) - Streptococcus salivarius (0/7) - Streptococcus mutans (0/7) - Escherichia coli (0/4) - Enterobacter aerogenes (0/1) - Salmonella enterica serovar Typhimurium (0/1)
Swiss-Prot Entry Q2QBT0
PDB Entry Unknown
Other databases EMBL DQ146939GO GO:0005576GO GO:0005102GO GO:0019835GO GO:0050830

InterPro IPR006079InterPro IPR000446Pfam PF02052PRINTS PR00324
Description Mode of action:
Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.

Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor. plasmid DNA. The sequences reported are absolutely identical.
[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44, POST-TRANSLATIONAL MODIFICATIONS, FUNCTION, AND MASS SPECTROMETRY, STRAIN=42.
PubMed=16461661;DOI=10.1128/AEM.72.2.1148-1156.2006
Wirawan R.E., Klesse N.A., Jack R.W., Tagg J.R.
"Molecular and genetic characterization of a novel nisin variant produced by Streptococcus uberis.", Appl. Environ. Microbiol. 72:1148-1156(2006).

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Sequence
........10........20........30........40
| | | |
ITSKSLCTPGCKTGILMTCPLKTATCGCHFG
Wheel representation
Composition
AA N° %

AA N° %

AA N° %
Ala 1 3.23%

Ile 2 6.45%

Arg 0 .00%
Cys 5 16.13%

Lys 3 9.68%

Ser 2 6.45%
Asp 0 .00%

Leu 3 9.68%

Thr 6 19.35%
Glu 0 .00%

Met 1 3.23%

Val 0 .00%
Phe 1 3.23%

Asn 0 .00%

Trp 0 .00%
Gly 4 12.90%

Pro 2 6.45%

Tyr 0 .00%
His 1 3.23%

Gln 0 .00%
Total 31
Formula C134 H226 N36 O40 S6
Absent amino acids DENQRVWY
Common amino acids T
Mass (Da) 3192.37
Net charge +4
Isoelectric point 8.51
Basic residues 4
Acidic residues 0
Hydrophobic residues 7
Polar residues 17
Aliphatic residues 5
Tiny residues 7
Boman Index -1.63
Hydropathy Index 45
Aliphatic Index 66.13
Instability Index 30.65 (stable)
Half Life Mammalian : 20 hour
Yeast : 30 min
E. coli : >10 hour
Extinction Coefficient 0 M-1 cm-1
Absorbance 280nm 8.33
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

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