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View bacteriocin : Nisin Z

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Accession BAC049
Name Nisin Z
Related Entries Nisin ANisin QNisin Fnisin U
Gene nisZ
Class Lantibiotic
Producer Organism Lactococcus lactis subsp (Streptococcus lactis), lactis [Gram-positive]
Taxonomy BacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus
Target organisms active on Gram-positive bacteria: Enterococcus - Lactobacillus - Lactococcus - Leuconostoc - Listeria - clostridium
Swiss-Prot Entry P29559
PDB Entry 1WCO resolved by NMR
Other databases EMBL X61144EMBL D10768EMBL Z18947InterPro IPR006079InterPro IPR000446

Pfam 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.
[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=NIZO 22186
MEDLINE=92037612;PubMed=1935953;DOI=10.1111/j.1432-1033.1991.tb16317.x
Mulders J.W.M., Boerrigter I.J., Rollema H.S., Siezen R.J., de Vos W.M.
"Identification and characterization of the lantibiotic nisin Z, a natural nisin variant.", Eur. J. Biochem. 201:581-584(1991).

[Ref. 2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=JCM 7638
DOI=10.2323/jgam.38.271
Araya T., Ishibashi N., Shimamura S.
"Genetic evidence that Lactococcus lactis JCM7638 produces a mutated form of nisin.", J. Gen. Appl. Microbiol. 38:271-278(1992).

[Ref. 3] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=N8
MEDLINE=95352820;PubMed=7626780;
Immonen T., Ye S., Ra R., Qiao M., Paulin L., Saris P.E.J.
"The codon usage of the nisZ operon in Lactococcus lactis N8 suggests a non-lactococcal origin of the conjugative nisin-sucrose transposon.", DNA Seq. 5:203-218(1995).

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Sequence
 ........10 ........20 ........30 ........40 
          |          |          |          | 
 ITSISLCTPG CKTGALMGCN MKTATCNCSI HVSK

Annotations


FeaturePosition(s)LengthDescription
PEPTIDE1↔3434
Lantibiotic nisin-Z.
Feature identifier = PRO_0000017125.
Modified residue22,3-didehydrobutyrine.
Modified residue52,3-didehydroalanine (Ser).
Modified residue332,3-didehydroalanine (Ser).
Cross-link3↔75Lanthionine (Ser-Cys).
Cross-link8↔114Beta-methyllanthionine (Thr-Cys).
Cross-link13↔197Beta-methyllanthionine (Thr-Cys).
Cross-link23↔264Beta-methyllanthionine (Thr-Cys).
Cross-link25↔284Beta-methyllanthionine (Thr-Cys).
VARIANT27N -> H (Nisin A).
VARIANT30I -> V (Nisin F).
HELIX9↔124
TURN15↔173
Wheel representation
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3D Structure
Composition
Formula C141 H245 N41 O46 S7
Absent amino acids DEFQRWY
Common amino acids CT
Mass (Da) 3493.74
Net charge +4
Isoelectric point 8.51
Basic residues 4
Acidic residues 0
Hydrophobic residues 8
Polar residues 19
Aliphatic residues 6
Tiny residues 9
Boman Index -14.86
Hydropathy Index 0.41
Aliphatic Index 71.76
Instability Index 17.08 (stable)
Half Life Mammalian : 20 hour
Yeast : 30 min
E. coli : >10 hour
Extinction Coefficient 250 M-1 cm-1
Absorbance 280nm 7.58
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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