ID   LANNU_STRUB             Reviewed;          55 AA.
AC   Q2QBT0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Lantibiotic nisin-U;
DE   Flags: Precursor;
GN   Name=nsuA;
OS   Streptococcus uberis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1349;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44, DEHYDRATION
RP   AT THR-26; SER-29 AND THR-42, LANTHIONINE CROSS-LINKS, FUNCTION, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=42;
RX   PubMed=16461661; DOI=10.1128/aem.72.2.1148-1156.2006;
RA   Wirawan R.E., Klesse N.A., Jack R.W., Tagg J.R.;
RT   "Molecular and genetic characterization of a novel nisin variant produced
RT   by Streptococcus uberis.";
RL   Appl. Environ. Microbiol. 72:1148-1156(2006).
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. {ECO:0000269|PubMed:16461661}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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 (By similarity). {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=3029.0; Mass_error=0.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16461661};
CC   -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR   EMBL; DQ146939; ABA00878.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2QBT0; -.
DR   SMR; Q2QBT0; -.
DR   PRIDE; Q2QBT0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Lantibiotic; Secreted; Thioether bond.
FT   PROPEP          1..24
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT                   /id="PRO_0000326410"
FT   PEPTIDE         25..55
FT                   /note="Lantibiotic nisin-U"
FT                   /id="PRO_0000326411"
FT   MOD_RES         26
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT   MOD_RES         29
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT   MOD_RES         42
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT   CROSSLNK        27..31
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT   CROSSLNK        32..35
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT   CROSSLNK        37..43
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT   CROSSLNK        47..50
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:16461661"
FT   CROSSLNK        49..52
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:16461661"
SQ   SEQUENCE   55 AA;  5863 MW;  9BAD9B71254E0D5E CRC64;
     MNNEDFNLDL IKISKENNSG ASPRITSKSL CTPGCKTGIL MTCPLKTATC GCHFG