ID   LANA_STRPY              Reviewed;          51 AA.
AC   P36501;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Lantibiotic streptococcin A-FF22;
DE   AltName: Full=Antibacterial peptide SA-FF22;
DE   Flags: Precursor;
GN   Name=scnA;
OS   Streptococcus pyogenes.
OG   Plasmid.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FF22;
RX   PubMed=8328813; DOI=10.1128/aem.59.6.1969-1971.1993;
RA   Hynes W.L., Ferretti J.J., Tagg J.R.;
RT   "Cloning of the gene encoding Streptococcin A-FF22, a novel lantibiotic
RT   produced by Streptococcus pyogenes, and determination of its nucleotide
RT   sequence.";
RL   Appl. Environ. Microbiol. 59:1969-1971(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FF22;
RA   McLaughlin R.E., Hynes W.L.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 26-51, DEHYDRATION AT THR-48, AND LANTHIONINE
RP   CROSS-LINKS.
RC   STRAIN=FF22;
RX   PubMed=8125103; DOI=10.1111/j.1432-1033.1994.tb18643.x;
RA   Jack R.W., Carne A., Metzger J., Stefanovic S., Sahl H.-G., Jung G.,
RA   Tagg J.R.;
RT   "Elucidation of the structure of SA-FF22, a lanthionine-containing
RT   antibacterial peptide produced by Streptococcus pyogenes strain FF22.";
RL   Eur. J. Biochem. 220:455-462(1994).
CC   -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC       active on certain 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   -!- SUBCELLULAR LOCATION: Secreted. Cell surface. Note=Either cell
CC       associated or in a released extracellular form.
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   -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR   EMBL; AF026542; AAB92600.1; -; Genomic_DNA.
DR   PIR; T09004; T09004.
DR   RefSeq; WP_023612114.1; NZ_WVHC01000001.1.
DR   AlphaFoldDB; P36501; -.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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..25
FT                   /evidence="ECO:0000269|PubMed:8125103"
FT                   /id="PRO_0000017134"
FT   PEPTIDE         26..51
FT                   /note="Lantibiotic streptococcin A-FF22"
FT                   /id="PRO_0000017135"
FT   MOD_RES         48
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:8125103"
FT   CROSSLNK        33..38
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:8125103"
FT   CROSSLNK        35..49
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:8125103"
FT   CROSSLNK        42..50
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:8125103"
SQ   SEQUENCE   51 AA;  5666 MW;  77E378C7A1B9DAAC CRC64;
     MEKNNEVINS IQEVSLEELD QIIGAGKNGV FKTISHECHL NTWAFLATCC S