ID   LANG_STAGA              Reviewed;          52 AA.
AC   P21838;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Lantibiotic gallidermin;
DE   Flags: Precursor;
GN   Name=gdmA;
OS   Staphylococcus gallinarum.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1293;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TU 3928;
RX   PubMed=2765032; DOI=10.1016/0378-1097(89)90050-5;
RA   Schnell N., Entian K.-D., Goetz F., Hoerner T., Kellner R., Jung G.;
RT   "Structural gene isolation and prepeptide sequence of gallidermin, a new
RT   lanthionine containing antibiotic.";
RL   FEMS Microbiol. Lett. 49:263-267(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 31-52, DEHYDRATION AT THR-44, AND LANTHIONINE
RP   CROSS-LINKS.
RC   STRAIN=TU 3928;
RX   PubMed=3181159; DOI=10.1111/j.1432-1033.1988.tb14344.x;
RA   Kellner R., Jung G., Hoerner T., Zaehner H., Schnell N., Entian K.-D.,
RA   Goetz F.;
RT   "Gallidermin: a new lanthionine-containing polypeptide antibiotic.";
RL   Eur. J. Biochem. 177:53-59(1988).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=1932575; DOI=10.1002/bip.360310626;
RA   Freund S., Jung G., Gutbrod O., Folkers G., Gibbons W.A., Allgaier H.,
RA   Werner R.;
RT   "The solution structure of the lantibiotic gallidermin.";
RL   Biopolymers 31:803-811(1991).
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.
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. The C-terminal lanthionine undergoes decarboxylation.
CC       This is followed by membrane translocation and cleavage of the modified
CC       precursor.
CC   -!- PTM: The structure of the 2,3-didehydrobutyrine is not discussed in
CC       PubMed:1932575. However, in Fig. 5 the NMR model appears to have the Z-
CC       isomer.
CC   -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR   EMBL; U61158; AAB61135.1; -; Genomic_DNA.
DR   PIR; A61072; EPSGD.
DR   RefSeq; WP_042739435.1; NZ_JXCF01000013.1.
DR   AlphaFoldDB; P21838; -.
DR   TCDB; 1.C.20.1.2; the nisin (nisin) family.
DR   OrthoDB; 2089942at2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; IPR006079; Lantibiotic_typ-A_Bacillales.
DR   Pfam; PF02052; Gallidermin; 1.
DR   PRINTS; PR00323; GALLIDERMIN.
DR   TIGRFAMs; TIGR03731; lantibio_gallid; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; D-amino acid;
KW   Direct protein sequencing; Lantibiotic; Thioether bond.
FT   PROPEP          1..30
FT                   /evidence="ECO:0000269|PubMed:3181159"
FT                   /id="PRO_0000017118"
FT   PEPTIDE         31..52
FT                   /note="Lantibiotic gallidermin"
FT                   /id="PRO_0000017119"
FT   MOD_RES         44
FT                   /note="(Z)-2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:3181159"
FT   CROSSLNK        33..37
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:3181159"
FT   CROSSLNK        38..41
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:3181159"
FT   CROSSLNK        46..51
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:3181159"
FT   CROSSLNK        49..52
FT                   /note="S-(2-aminovinyl)-D-cysteine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:3181159"
SQ   SEQUENCE   52 AA;  5647 MW;  8584C0040AB4786D CRC64;
     MEAVKEKNEL FDLDVKVNAK ESNDSGAEPR IASKFLCTPG CAKTGSFNSY CC