ID   LANZ_LACLL              Reviewed;          57 AA.
AC   P29559;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-SEP-2026, entry version 92.
DE   RecName: Full=Lantibiotic nisin-Z;
DE   Flags: Precursor;
GN   Name=nisZ;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NIZO 22186;
RX   PubMed=1935953; DOI=10.1111/j.1432-1033.1991.tb16317.x;
RA   Mulders J.W.M., Boerrigter I.J., Rollema H.S., Siezen R.J., de Vos W.M.;
RT   "Identification and characterization of the lantibiotic nisin Z, a natural
RT   nisin variant.";
RL   Eur. J. Biochem. 201:581-584(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CIP 103449 / JCM 7638;
RA   Araya T., Ishibashi N., Shimamura S.;
RT   "Genetic evidence that Lactococcus lactis JCM7638 produces a mutated form
RT   of nisin.";
RL   J. Gen. Appl. Microbiol. 38:271-278(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N8;
RX   PubMed=7626780; DOI=10.3109/10425179509030968;
RA   Immonen T., Ye S., Ra R., Qiao M., Paulin L., Saris P.E.J.;
RT   "The codon usage of the nisZ operon in Lactococcus lactis N8 suggests a
RT   non-lactococcal origin of the conjugative nisin-sucrose transposon.";
RL   DNA Seq. 5:203-218(1995).
RN   [4]
RP   STRUCTURE BY NMR OF 24-57, DEHYDRATION AT THR-25; SER-28 AND SER-56, AND
RP   LANTHIONINE CROSS-LINKS.
RX   PubMed=15361862; DOI=10.1038/nsmb830;
RA   Hsu S.T., Breukink E., Tischenko E., Lutters M.A., de Kruijff B.,
RA   Kaptein R., Bonvin A.M., van Nuland N.A.;
RT   "The nisin-lipid II complex reveals a pyrophosphate cage that provides a
RT   blueprint for novel antibiotics.";
RL   Nat. Struct. Mol. Biol. 11:963-967(2004).
CC   -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC       active on Gram-positive bacteria. The bactericidal activity of
CC       lantibiotics is based on depolarization of energized bacterial
CC       cytoplasmic membranes, initiated by the formation of aqueous
CC       transmembrane pores.
CC   -!- PTM: Maturation of lantibiotics involves the enzymatic conversion of
CC       Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC       with cysteine. This is followed by membrane translocation and cleavage
CC       of the modified precursor.
CC   -!- PTM: The structure of the 2,3-didehydrobutyrine is not discussed in
CC       PubMed:15361862. It is probably the Z-isomer by similarity.
CC   -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR   EMBL; X61144; CAA43440.1; -; Genomic_DNA.
DR   EMBL; D10768; BAA01598.1; -; Genomic_DNA.
DR   EMBL; Z18947; CAA79467.1; -; Genomic_DNA.
DR   RefSeq; WP_015425978.1; NZ_AP038894.1.
DR   PDB; 1WCO; NMR; -; N=24-57.
DR   PDB; 6M7Y; X-ray; 2.79 A; C/D=2-35.
DR   AlphaFoldDB; P29559; -.
DR   BMRB; P29559; -.
DR   SMR; P29559; -.
DR   DrugBank; DB07780; Farnesyl diphosphate.
DR   EvolutionaryTrace; P29559; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR   InterPro; IPR006079; Lantibiotic_typ-A_Bacillales.
DR   NCBIfam; TIGR03731; lantibio_gallid; 1.
DR   Pfam; PF02052; Gallidermin; 1.
DR   PRINTS; PR00324; NISIN.
DR   PDBsum; 1WCO; -.
DR   PDBsum; 6M7Y; -.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Lantibiotic;
KW   Thioether bond.
FT   PROPEP          1..23
FT                   /id="PRO_0000017124"
FT   PEPTIDE         24..57
FT                   /note="Lantibiotic nisin-Z"
FT                   /id="PRO_0000017125"
FT   MOD_RES         25
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   MOD_RES         28
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   MOD_RES         56
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   CROSSLNK        26..30
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   CROSSLNK        31..34
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   CROSSLNK        36..42
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   CROSSLNK        46..49
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   CROSSLNK        48..51
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15361862"
FT   VARIANT         50
FT                   /note="N -> H (in strain: JCM 7638)"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:6M7Y"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:1WCO"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:1WCO"
SQ   SEQUENCE   57 AA;  5940 MW;  DF5E4428AC70BFEF CRC64;
     MSTKDFNLDL VSVSKKDSGA SPRITSISLC TPGCKTGALM GCNMKTATCN CSIHVSK
//