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1.C.20.1.2
Class I lantibiotic bacteriocin Gallidermin precursor (has a mersacidin-like Lipid II domain, and forms Lipid II-dependent pores) (Sahl and Bierbaum, 1998). The genetic organization, biosynthesis, modification, excretion, extracellular activation of the modified pre-peptide by proteolytic processing, self-protection of the producer, gene regulation, structure, and mode of action have been reviewed (Götz et al. 2014). The Gallidermin-lipid II complex probably forms water pores in the membrane (Pokhrel et al. 2019). It complexes Lipid II more tightly than it forms transmembrane channels (Pokhrel et al. 2021).

Accession Number:P21838
Protein Name:LANG aka GDMA
Length:52
Molecular Weight:5647.00
Species:Staphylococcus gallinarum [1293]
Location1 / Topology2 / Orientation3: Secreted1
Substrate

Cross database links:

Pfam: PF02052   

Gene Ontology

GO:0005102 F:receptor binding
GO:0019835 P:cytolysis
GO:0050830 P:defense response to Gram-positive bacterium

References (3)

[1] “Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic.”  Schnell N.et.al.   2765032
[2] “Gallidermin: a new lanthionine-containing polypeptide antibiotic.”  Kellner R.et.al.   3181159
[3] “The solution structure of the lantibiotic gallidermin.”  Freund S.et.al.   1932575

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FASTA formatted sequence
1:	MEAVKEKNEL FDLDVKVNAK ESNDSGAEPR IASKFLCTPG CAKTGSFNSY CC