Bacteriocin: gallidermin
Accession: BAC018
Classification
Class: Lantibiotic
Genetics
Gene: gdmA
Producer and target organisms
Producer Organism: Staphylococcus gallinarum [Gram-positive]
Description
Mode of action:
Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The C-terminal lanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor.
Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The C-terminal lanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor.
Uniprot and PDB links
UniProt Entry: P21838
PDB EntryUnknown
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=TU 3928
MEDLINE=89306540;PubMed=2765032;DOI=10.1016/0378-1097(89)90050-5
Schnell N., Entian K.-D., Goetz F., Hoerner T., Kellner R., Jung G.
"Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic.", FEMS Microbiol. Lett. 49:263-267(1989).
MEDLINE=89306540;PubMed=2765032;DOI=10.1016/0378-1097(89)90050-5
Schnell N., Entian K.-D., Goetz F., Hoerner T., Kellner R., Jung G.
"Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic.", FEMS Microbiol. Lett. 49:263-267(1989).
PROTEIN SEQUENCE OF 31-52, STRAIN=TU 3928
MEDLINE=89030695;PubMed=3181159;
Kellner R., Jung G., Hoerner T., Zaehner H., Schnell N., Entian K.-D., Goetz F.
"Gallidermin: a new lanthionine-containing polypeptide antibiotic.", Eur. J. Biochem. 177:53-59(1988).
MEDLINE=89030695;PubMed=3181159;
Kellner R., Jung G., Hoerner T., Zaehner H., Schnell N., Entian K.-D., Goetz F.
"Gallidermin: a new lanthionine-containing polypeptide antibiotic.", Eur. J. Biochem. 177:53-59(1988).
STRUCTURE BY NMR.
MEDLINE=92032577;PubMed=1932575;
Freund S., Jung G., Gutbrod O., Folkers G., Gibbons W.A., Allgaier H., Werner R.
"The solution structure of the lantibiotic gallidermin.", Biopolymers 31:803-811(1991).
MEDLINE=92032577;PubMed=1932575;
Freund S., Jung G., Gutbrod O., Folkers G., Gibbons W.A., Allgaier H., Werner R.
"The solution structure of the lantibiotic gallidermin.", Biopolymers 31:803-811(1991).
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Gene structure
| Gene id | Name | Description | Location |
| BACGene38 | gdmE | GdmE proposed ABC transporter subunit (integral membrane domain) | complement(1..177) |
| BACGene39 | gdmF | GdmF proposed ABC transporter subunit (ATP-binding domain) | complement(179..874) |
| BACGene40 | gdmH | GdmH putative membrane protein | 1035..2027 |
| BACGene41 | gdmT | GdmT ABC transporter | complement(2043..3686) |
| BACGene42 | gdmA | GdmA precursor peptide of the lanthionine-containing peptide antibiotic (lantibiotic)gallidermin | 3844..4002 |
| BACGene43 | gdmB | GdmB modifying enzyme; 5' end | 4068..4373 |
Protein sequence
| ........10 ........20 ........30 | | | IASKFLCTPG CAKTGSFNSY CC |
Wheel representation
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔22 | 22 | Lantibiotic gallidermin. Feature identifier = PRO_0000017119. |
| Modified residue | 14 | (Z)-2,3-didehydrobutyrine. | |
| Cross-link | 3↔7 | 5 | Lanthionine (Ser-Cys). |
| Cross-link | 8↔11 | 4 | Beta-methyllanthionine (Thr-Cys). |
| Cross-link | 16↔21 | 6 | Lanthionine (Ser-Cys). |
| Cross-link | 19↔22 | 4 | S-(2-aminovinyl)-D-cysteine (Ser-Cys). |
Composition
Hydrophobicity
Composition
| Formula | C99
H153
N25
O30
S4 |
| Absent amino acids | DEHMQRVW |
| Common amino acids | C |
| Mass (Da) | 2320.05 |
| Net charge | +2 |
| Isoelectric point | 8.33 |
| Basic residues | 2 |
| Acidic residues | 0 |
| Hydrophobic residues | 6 |
| Polar residues | 13 |
| Aliphatic residues | 2 |
| Tiny residues | 7 |
| Boman Index | -6.8 |
| Hydropathy Index | 0.4 |
| Aliphatic Index | 44.55 |
| Instability Index | 20.5 (stable) |
| Half Life |
Mammalian : 20 hour Yeast : 30 min E. coli : >10 hour |
| Extinction Coefficient | 1740 M-1 cm-1 |
| Absorbance 280nm | 82.86 |
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