ID   CINA_STRGV              Reviewed;          78 AA.
AC   P29827;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Lantibiotic cinnamycin;
DE   AltName: Full=Lanthiopeptin;
DE   AltName: Full=Lantibiotic Ro 09-0198;
DE   Flags: Precursor;
GN   Name=cinA; Synonyms=rocA;
OS   Streptomyces griseoverticillatus (Streptoverticillium griseoverticillatum).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces cinnamoneus group.
OX   NCBI_TaxID=68215;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MAR 164C-MY6;
RX   PubMed=2070795; DOI=10.1111/j.1432-1033.1991.tb16138.x;
RA   Kaletta C., Entian K.-D., Jung G.;
RT   "Prepeptide sequence of cinnamycin (Ro 09-0198): the first structural gene
RT   of a duramycin-type lantibiotic.";
RL   Eur. J. Biochem. 199:411-415(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 60-78.
RX   PubMed=2125590; DOI=10.7164/antibiotics.43.1403;
RA   Fredenhagen A., Fendrich G., Marki F., Marki W., Gruner J., Raschdorf F.,
RA   Peter H.H.;
RT   "Duramycins B and C, two new lanthionine containing antibiotics as
RT   inhibitors of phospholipase A2. Structural revision of duramycin and
RT   cinnamycin.";
RL   J. Antibiot. 43:1403-1412(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 60-78, AND HYDROXYLATION AT ASP-74.
RX   PubMed=2544544; DOI=10.7164/antibiotics.42.837;
RA   Naruse N., Tenmyo O., Tomita K., Konishi M., Miyaki T., Kawaguchi H.,
RA   Fukase K., Wakamiya T., Shiba T.;
RT   "Lanthiopeptin, a new peptide antibiotic. Production, isolation and
RT   properties of lanthiopeptin.";
RL   J. Antibiot. 42:837-845(1989).
CC   -!- FUNCTION: Can act as inhibitor of the enzyme phospholipase A2, and of
CC       the angiotensin-converting enzyme. Shows inhibitory activities against
CC       herpes simplex virus and immunopotentiating activities. Its
CC       antimicrobial activities are not very pronounced.
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   EMBL; X58545; CAA41436.1; -; Genomic_DNA.
DR   PIR; A45767; EWSMCN.
DR   PIR; S17181; EWSMYG.
DR   PDB; 2DDE; NMR; -; A=60-78.
DR   PDBsum; 2DDE; -.
DR   AlphaFoldDB; P29827; -.
DR   SMR; P29827; -.
DR   DrugBank; DB04731; 1-ACETYL-2-LYSO-SN-GLYCERO-3-PHOSPHOETHANOLAMINE.
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; IPR046016; DUF5973.
DR   Pfam; PF19398; DUF5973; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW   Direct protein sequencing; Hydroxylation; Lantibiotic; Thioether bond.
FT   PROPEP          1..59
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000017148"
FT   PEPTIDE         60..78
FT                   /note="Lantibiotic cinnamycin"
FT                   /id="PRO_0000017149"
FT   MOD_RES         74
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000269|PubMed:2544544"
FT   CROSSLNK        60..77
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT   CROSSLNK        63..73
FT                   /note="Lanthionine (Ser-Cys)"
FT   CROSSLNK        64..70
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT   CROSSLNK        65..78
FT                   /note="Lysinoalanine (Ser-Lys)"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:2DDE"
SQ   SEQUENCE   78 AA;  8205 MW;  0ACDAE6BA54E5E7A CRC64;
     MTASILQQSV VDADFRAALL ENPAAFGASA AALPTPVEAQ DQASLDFWTK DIAATEAFAC
     RQSCSFGPFT FVCDGNTK