ID   LANC_STRS6              Reviewed;          19 AA.
AC   P38655;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Lantibiotic ancovenin;
OS   Streptomyces sp. (strain A647P-2).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=72591;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Wakamiya T., Ueki Y., Shiba T., Kido Y., Motoki Y.;
RT   "The structure of ancovenin, a new peptide inhibitor of angiotensin I
RT   converting enzyme.";
RL   Tetrahedron Lett. 26:665-668(1985).
CC   -!- FUNCTION: Acts as an inhibitor of angiotensin I converting enzyme.
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 or the formation of dialkylamine bonds with lysine. This
CC       is followed by membrane translocation and cleavage of the modified
CC       precursor.
CC   -!- SIMILARITY: Belongs to the type B lantibiotic family. {ECO:0000305}.
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DR   PIR; A61284; EWSMAN.
DR   AlphaFoldDB; P38655; -.
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.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Lantibiotic; Thioether bond.
FT   PEPTIDE         1..19
FT                   /note="Lantibiotic ancovenin"
FT                   /id="PRO_0000043968"
FT   CROSSLNK        1..18
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT   CROSSLNK        4..14
FT                   /note="Lanthionine (Ser-Cys)"
FT   CROSSLNK        5..11
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT   CROSSLNK        6..19
FT                   /note="Lysinoalanine (Ser-Lys)"
SQ   SEQUENCE   19 AA;  2033 MW;  F434299E2736286A CRC64;
     CVQSCSFGPL TWSCDGNTK