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Protein

Lantibiotic nisin-Z

Gene

nisZ

Organism
Lactococcus lactis subsp. lactis (Streptococcus lactis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic nisin-Z
Gene namesi
Name:nisZ
OrganismiLactococcus lactis subsp. lactis (Streptococcus lactis)
Taxonomic identifieri1360 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 2323PRO_0000017124Add
BLAST
Peptidei24 – 5734Lantibiotic nisin-ZPRO_0000017125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 2512,3-didehydrobutyrine
Cross-linki26 ↔ 30Lanthionine (Ser-Cys)
Modified residuei28 – 2812,3-didehydroalanine (Ser)
Cross-linki31 ↔ 34Beta-methyllanthionine (Thr-Cys)
Cross-linki36 ↔ 42Beta-methyllanthionine (Thr-Cys)
Cross-linki46 ↔ 49Beta-methyllanthionine (Thr-Cys)
Cross-linki48 ↔ 51Beta-methyllanthionine (Thr-Cys)
Modified residuei56 – 5612,3-didehydroalanine (Ser)

Post-translational modificationi

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.
The structure of the 2,3-didehydrobutyrine is not discussed in PubMed:15361862. It is probably the Z-isomer by similarity.

Keywords - PTMi

Thioether bond

Structurei

Secondary structure

1
57
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 354Combined sources
Turni38 – 403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WCONMR-N24-57[»]
ProteinModelPortaliP29559.
SMRiP29559. Positions 28-56.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29559.

Family & Domainsi

Sequence similaritiesi

Belongs to the type A lantibiotic family.Curated

Family and domain databases

InterProiIPR006079. Lantibiotic_typ-A_Bacillales.
[Graphical view]
PfamiPF02052. Gallidermin. 1 hit.
[Graphical view]
PRINTSiPR00324. NISIN.
TIGRFAMsiTIGR03731. lantibio_gallid. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29559-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKDFNLDL VSVSKKDSGA SPRITSISLC TPGCKTGALM GCNMKTATCN

CSIHVSK
Length:57
Mass (Da):5,940
Last modified:April 1, 1993 - v1
Checksum:iDF5E4428AC70BFEF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501N → H in strain: JCM 7638.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61144 Genomic DNA. Translation: CAA43440.1.
D10768 Genomic DNA. Translation: BAA01598.1.
Z18947 Genomic DNA. Translation: CAA79467.1.
RefSeqiWP_015425978.1. NZ_LKLQ01000010.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61144 Genomic DNA. Translation: CAA43440.1.
D10768 Genomic DNA. Translation: BAA01598.1.
Z18947 Genomic DNA. Translation: CAA79467.1.
RefSeqiWP_015425978.1. NZ_LKLQ01000010.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WCONMR-N24-57[»]
ProteinModelPortaliP29559.
SMRiP29559. Positions 28-56.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP29559.

Family and domain databases

InterProiIPR006079. Lantibiotic_typ-A_Bacillales.
[Graphical view]
PfamiPF02052. Gallidermin. 1 hit.
[Graphical view]
PRINTSiPR00324. NISIN.
TIGRFAMsiTIGR03731. lantibio_gallid. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification and characterization of the lantibiotic nisin Z, a natural nisin variant."
    Mulders J.W.M., Boerrigter I.J., Rollema H.S., Siezen R.J., de Vos W.M.
    Eur. J. Biochem. 201:581-584(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NIZO 22186.
  2. "Genetic evidence that Lactococcus lactis JCM7638 produces a mutated form of nisin."
    Araya T., Ishibashi N., Shimamura S.
    J. Gen. Appl. Microbiol. 38:271-278(1992)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: JCM 7638.
  3. "The codon usage of the nisZ operon in Lactococcus lactis N8 suggests a non-lactococcal origin of the conjugative nisin-sucrose transposon."
    Immonen T., Ye S., Ra R., Qiao M., Paulin L., Saris P.E.J.
    DNA Seq. 5:203-218(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: N8.
  4. "The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics."
    Hsu S.T., Breukink E., Tischenko E., Lutters M.A., de Kruijff B., Kaptein R., Bonvin A.M., van Nuland N.A.
    Nat. Struct. Mol. Biol. 11:963-967(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-57, DISULFIDE BONDS.

Entry informationi

Entry nameiLANZ_LACLL
AccessioniPrimary (citable) accession number: P29559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: March 16, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.