ID   LANNA_STASI             Reviewed;          57 AA.
AC   E0WX65;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Lantibiotic nukacin {ECO:0000250|UniProtKB:Q9KWM4};
DE   AltName: Full=Nukacin 3299 {ECO:0000303|PubMed:20627619};
DE   AltName: Full=Simulancin 3299 {ECO:0000303|PubMed:20627619, ECO:0000312|EMBL:ACU82391.1};
DE   Flags: Precursor;
GN   Name=nukA {ECO:0000250|UniProtKB:Q9KWM4};
OS   Staphylococcus simulans.
OG   Plasmid pRJ97 {ECO:0000269|PubMed:20627619}.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1286;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACU82391.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-37,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC   STRAIN=3299 {ECO:0000269|PubMed:20627619};
RX   PubMed=20627619; DOI=10.1016/j.vetmic.2010.04.032;
RA   Ceotto H., Holo H., da Costa K.F.S., Nascimento J.S., Salehian Z., Nes I.,
RA   Bastos M.C.F.;
RT   "Nukacin 3299, a lantibiotic produced by Staphylococcus simulans 3299
RT   identical to nukacin ISK-1.";
RL   Vet. Microbiol. 146:124-131(2010).
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 (By similarity). {ECO:0000250|UniProtKB:Q9KWM4}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pHs for antimicrobial activity are 3.0 and 6.0. Activity is
CC         reduced by 50% at alkaline pHs 9.0 and 11.0.
CC         {ECO:0000269|PubMed:20627619};
CC       Temperature dependence:
CC         No change in antimicrobial activity between 80 or 100 degrees Celsius
CC         after 15 minutes, but reduction in 50% antimicrobial activity at 121
CC         degrees Celsius after 15 minutes. {ECO:0000269|PubMed:20627619};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9KWM4}.
CC       Note=Through the specific ABC transporter nukT.
CC       {ECO:0000250|UniProtKB:Q9KWM4}.
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).
CC       {ECO:0000250|UniProtKB:Q9KWM4}.
CC   -!- MASS SPECTROMETRY: Mass=2957.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20627619};
CC   -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000255}.
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DR   EMBL; GQ380548; ACU82391.1; -; Genomic_DNA.
DR   RefSeq; WP_011152951.1; NZ_QXVW01000024.1.
DR   AlphaFoldDB; E0WX65; -.
DR   SMR; E0WX65; -.
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; IPR007682; Lantibiotic_typ-A_Lactobact.
DR   Pfam; PF04604; L_biotic_typeA; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Lantibiotic; Plasmid; Secreted; Thioether bond.
FT   PROPEP          1..30
FT                   /evidence="ECO:0000269|PubMed:20627619"
FT                   /id="PRO_0000408771"
FT   PEPTIDE         31..57
FT                   /note="Lantibiotic nukacin"
FT                   /evidence="ECO:0000269|PubMed:20627619"
FT                   /id="PRO_0000408772"
FT   MOD_RES         54
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KWM4"
FT   CROSSLNK        39..44
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KWM4"
FT   CROSSLNK        41..55
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KWM4"
FT   CROSSLNK        48..56
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KWM4"
SQ   SEQUENCE   57 AA;  6403 MW;  9BF0046242995426 CRC64;
     MENSKVMKDI EVANLLEEVQ EDELNEVLGA KKKSGVIPTV SHDCHMNSFQ FVFTCCS