LANZ_LACLL
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 25-MAY-2022, entry version 86.
DE RecName: Full=Lantibiotic nisin-Z;
DE Flags: Precursor;
GN Name=nisZ;
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC Bacteria; Firmicutes; 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_QYRO01000015.1.
DR PDB; 1WCO; NMR; -; N=24-57.
DR PDB; 6M7Y; X-ray; 2.79 A; C/D=2-35.
DR PDBsum; 1WCO; -.
DR PDBsum; 6M7Y; -.
DR AlphaFoldDB; P29559; -.
DR BMRB; P29559; -.
DR SMR; P29559; -.
DR DrugBank; DB07780; Farnesyl diphosphate.
DR GeneID; 60356721; -.
DR GeneID; 66441584; -.
DR EvolutionaryTrace; P29559; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR006079; Lantibiotic_typ-A_Bacillales.
DR Pfam; PF02052; Gallidermin; 1.
DR PRINTS; PR00324; NISIN.
DR TIGRFAMs; TIGR03731; lantibio_gallid; 1.
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
