ID   LANPA_PAEPO             Reviewed;          53 AA.
AC   P86013; M1FLQ2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 2.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Lantibiotic paenibacillin {ECO:0000303|PubMed:17071789};
DE   Flags: Precursor;
GN   Name=paenA {ECO:0000312|EMBL:AFS60100.1};
OS   Paenibacillus polymyxa (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OSY-DF;
RA   Huang E., Yousef A.E.;
RT   "Biosynthesis of the antimicrobial peptide paenibacillin in Paenibacillus
RT   polymyxa OSY-DF.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, POST-TRANSLATIONAL
RP   MODIFICATIONS, AND MASS SPECTROMETRY.
RC   STRAIN=OSY-DF {ECO:0000269|PubMed:17071789};
RX   PubMed=17071789; DOI=10.1128/aem.02023-06;
RA   He Z., Kisla D., Zhang L., Yuan C., Green-Church K.B., Yousef A.E.;
RT   "Isolation and identification of a Paenibacillus polymyxa strain that
RT   coproduces a novel lantibiotic and polymyxin.";
RL   Appl. Environ. Microbiol. 73:168-178(2007).
RN   [3]
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, STRUCTURE BY NMR OF 24-53,
RP   ACETYLATION AT ALA-24, DEHYDRATION AT SER-25; THR-29; THR-30 AND SER-50,
RP   AND LANTHIONINE CROSS-LINKS.
RC   STRAIN=OSY-DF {ECO:0000269|PubMed:18625234};
RX   PubMed=18625234; DOI=10.1016/j.febslet.2008.07.008;
RA   He Z., Yuan C., Zhang L., Yousef A.E.;
RT   "N-terminal acetylation in paenibacillin, a novel lantibiotic.";
RL   FEBS Lett. 582:2787-2792(2008).
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. Lacks antibacterial activity against Gram-negative
CC       bacteria. {ECO:0000269|PubMed:17071789}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17071789,
CC       ECO:0000269|PubMed:18625234}.
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. {ECO:0000269|PubMed:17071789}.
CC   -!- PTM: The structure of the 2,3-didehydrobutyrines is not discussed in
CC       PubMed:17071789.
CC   -!- MASS SPECTROMETRY: Mass=2983.54; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17071789, ECO:0000269|PubMed:18625234};
CC   -!- MASS SPECTROMETRY: Mass=2983.44; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17071789, ECO:0000269|PubMed:18625234};
CC   -!- MASS SPECTROMETRY: Mass=2984.61; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17071789, ECO:0000269|PubMed:18625234};
CC   -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000255}.
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DR   EMBL; JQ728481; AFS60100.1; -; Genomic_DNA.
DR   AlphaFoldDB; P86013; -.
DR   iPTMnet; P86013; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Acetylation; Antibiotic; Antimicrobial; Bacteriocin;
KW   Direct protein sequencing; Lantibiotic; Secreted; Thioether bond.
FT   PROPEP          1..24
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000450323"
FT   PEPTIDE         24..53
FT                   /note="Lantibiotic paenibacillin"
FT                   /evidence="ECO:0000269|PubMed:17071789"
FT                   /id="PRO_0000352649"
FT   MOD_RES         24
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   MOD_RES         25
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   MOD_RES         29
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   MOD_RES         30
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   MOD_RES         50
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   CROSSLNK        34..38
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   CROSSLNK        40..43
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   CROSSLNK        42..45
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   CROSSLNK        46..49
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:18625234"
FT   CROSSLNK        48..52
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:18625234"
SQ   SEQUENCE   53 AA;  5819 MW;  DC8BCD3C2E52580C CRC64;
     MKVDQMFDLD LRKSYEASEL SPQASIIKTT IKVSKAVCKT LTCICTGSCS NCK