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7  structures 25  species 0  interactions 27  sequences 2  architectures

Family: Gallidermin (PF02052)

Summary: Gallidermin

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This is the Wikipedia entry entitled "Lantibiotics". More...

Lantibiotics Edit Wikipedia article

OPM superfamily161
OPM protein1mqy

Lantibiotics are a class of polycyclic peptide antibiotics that contain the characteristic thioether amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine, and 2-aminoisobutyric acid.

Lanthionine is composed of two alanine residues that are crosslinked on their β-carbon atoms by a thioether (monosulfide) linkage.

Lantibiotics are produced by a large number of Gram-positive bacteria such as Streptococcus and Streptomyces to attack other Gram-positive bacteria, and as such, they are considered a member of the bacteriocins. Bacteriocins are classified according to their extent of posttranslational modification. The lantibiotics are a class of more extensively modified bacteriocins, also called Class I bacteriocins. (Bacteriocins for which disulfide bonds are the only modification to the peptide are Class II bacteriocins.)

Lantibiotics are well studied because of the commercial use of these bacteria in the food industry for making dairy products such as cheese.

Nisin and epidermin are members of a family of lantibiotics that bind to lipid II, a cell wall precursor lipid component of target bacteria and disrupt cell wall production. The duramycin family of lantibiotics binds phosphoethanolamine in the membranes of its target cells and seem to disrupt several physiological functions.


The name lantibiotics was introduced in 1988 as an abbreviation for "lanthionine-containing peptide antibiotics".[1] The first structures of these antimicrobial agents were produced by pioneering work by Gross and Morell in the late 1960s and early 1970s, thus marking the formal introduction of lantibiotics. Since then, lantibiotics such as nisin have been used auspiciously for food preservation and have yet to encounter significant bacterial resistance. These attributes of lantibiotics have led to more detailed research into their structures and biosynthetic pathways.


Some contain 2 peptides, e.g. haloduracin.[6]


Lantibiotic Type # of
# of
thioether links
links[clarification needed]
A 34 5 0
A 21 3 1 [2]
mersacidin B 20 4 [3]
actagardine B 19 4 0
B 19 3 1 [5]
Sublancin 168 ? 37 1 2 [7]
Plantaricin C B 27 4 0

(Sublancin may be an S-linked glycopeptide.[8]


They are synthesised with a leader polypeptide sequence that is removed only during the transport of the molecule out of the synthesising cell. They are synthesized by ribosomes, which distinguishes them from most natural antibiotics.[9] There are four known enzymes (lanthipeptide synthetases) responsible for producing lanthionine rings.[10][11]

Mechanism of action

Lantibiotics show substantial specificity for some components (e.g., lipid II) of bacterial cell membranes especially of Gram-positive bacteria. Type A lantibiotics kill rapidly by pore formation, type B lantibiotics inhibit peptidoglycan biosynthesis.[12] They are active in very low concentrations.[13]


Food preservation

Lantibiotics are produced by Gram-positive bacteria and show strong antimicrobial action toward a wide range of other Gram-positive bacteria.[14] As such, they have become attractive candidates for use in food preservation (by inhibiting pathogens that cause food spoilage) and the pharmaceutical industry (to prevent or fight infections in humans or animals).[14]

Veterinary antibiotic

Duramycin is used for chickens.

Clinical antibiotic

One type known as B lantibiotic NVB302 entered phase 1 clinical trials in 2011 for use against Clostridium difficile,[15] and reported good results in 2012.[16]


BACTIBASE is an open-access database for bacteriocins including lantibiotics.[17][18] LANTIBASE is a lantibiotic specific resource.[19]


  1. ^ Chatterjee C, Paul M, Xie L, van der Donk WA (February 2005). "Biosynthesis and mode of action of lantibiotics". Chem. Rev. 105 (2): 633–84. doi:10.1021/cr030105v. PMID 15700960.
  2. ^ a b Kellner R, Jung G, Hörner T, Zähner H, Schnell N, Entian KD, Götz F (October 1988). "Gallidermin: a new lanthionine-containing polypeptide antibiotic". Eur. J. Biochem. 177 (1): 53–9. doi:10.1111/j.1432-1033.1988.tb14344.x. PMID 3181159.
  3. ^ a b Sass P, Jansen A, Szekat C, Sass V, Sahl HG, Bierbaum G (2008). "The lantibiotic mersacidin is a strong inducer of the cell wall stress response of Staphylococcus aureus". BMC Microbiol. 8: 186. doi:10.1186/1471-2180-8-186. PMC 2592248. PMID 18947397.
  4. ^ Brötz H, Bierbaum G, Markus A, Molitor E, Sahl HG (March 1995). "Mode of action of the lantibiotic mersacidin: inhibition of peptidoglycan biosynthesis via a novel mechanism?". Antimicrob. Agents Chemother. 39 (3): 714–9. doi:10.1128/AAC.39.3.714. PMC 162610. PMID 7793878.
  5. ^ a b Makino A, Baba T, Fujimoto K, Iwamoto K, Yano Y, Terada N, Ohno S, Sato SB, Ohta A, Umeda M, Matsuzaki K, Kobayashi T (January 2003). "Cinnamycin (Ro 09-0198) promotes cell binding and toxicity by inducing transbilayer lipid movement". J. Biol. Chem. 278 (5): 3204–9. doi:10.1074/jbc.M210347200. PMID 12446685.
  6. ^ Cooper LE, McClerren AL, Chary A, van der Donk WA (October 2008). "Structure-activity relationship studies of the two-component lantibiotic haloduracin". Chem. Biol. 15 (10): 1035–45. doi:10.1016/j.chembiol.2008.07.020. PMC 2633096. PMID 18940665.
  7. ^ Stein T (May 2005). "Bacillus subtilis antibiotics: structures, syntheses and specific functions". Mol. Microbiol. 56 (4): 845–57. doi:10.1111/j.1365-2958.2005.04587.x. PMID 15853875.
  8. ^ Oman TJ, Boettcher JM, Wang H, Okalibe XN, van der Donk WA (February 2011). "Sublancin is not a lantibiotic but an S-linked glycopeptide". Nat. Chem. Biol. 7 (2): 78–80. doi:10.1038/nchembio.509. PMC 3060661. PMID 21196935.
  9. ^ Siegers K, Heinzmann S, Entian KD (May 1996). "Biosynthesis of lantibiotic nisin. Posttranslational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex". J. Biol. Chem. 271 (21): 12294–301. doi:10.1074/jbc.271.21.12294. PMID 8647829.
  10. ^ Goto, Y; Li, B; Claesen, J; Shi, Y; Bibb, MJ; van der Donk, WA (2010). "Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights". PLoS Biology. 8 (3): e1000339. doi:10.1371/journal.pbio.1000339. PMC 2843593. PMID 20351769.
  11. ^ Zhang, Q; Yu, Y; Vélasquez, JE; van der Donk, WA (2012). "Evolution of lanthipeptide synthetases". Proceedings of the National Academy of Sciences. 109 (45): 18361–6. doi:10.1073/pnas.1210393109. PMC 3494888. PMID 23071302.
  12. ^ Brötz H, Sahl HG (2000). "New insights into the mechanism of action of lantibiotics—diverse biological effects by binding to the same molecular target". Journal of Antimicrobial Chemotherapy. 46 (1): 1–6. doi:10.1093/jac/46.1.1. PMID 10882681.
  13. ^ Cotter, Hill, Ross (2005). "Bacterial Lantibiotics: Strategies to Improve Therapeutic Potential" (PDF). 6. Current Protein and Peptide Science: 61–75. Cite journal requires |journal= (help)CS1 maint: multiple names: authors list (link)
  14. ^ a b van Kraaij C, de Vos WM, Siezen RJ, Kuipers OP (October 1999). "Lantibiotics: biosynthesis, mode of action and applications". Nat Prod Rep. 16 (5): 575–87. CiteSeerX doi:10.1039/a804531c. PMID 10584332.
  15. ^ "New antibiotic compound enters phase I clinical trial". Press Release. Wellcome Trust. 2011-11-03.
  16. ^ Parker S (2012-08-06). "Novacta Biosystems Limited completes Phase I study of NVB302 against C. difficile infection in healthy volunteers". Press Release. Celtic Pharma Holding.
  17. ^ Hammami R, Zouhir A, Ben Hamida J, Fliss I (2007). "BACTIBASE: a new web-accessible database for bacteriocin characterization". BMC Microbiology. 7: 89. doi:10.1186/1471-2180-7-89. PMC 2211298. PMID 17941971.
  18. ^ Hammami R, Zouhir A, Le Lay C, Ben Hamida J, Fliss I (2010). "BACTIBASE second release: a database and tool platform for bacteriocin characterization". BMC Microbiology. 10: 22. doi:10.1186/1471-2180-10-22. PMC 2824694. PMID 20105292.
  19. ^ "Archived copy". Archived from the original on 2013-08-15. Retrieved 2013-07-25.CS1 maint: archived copy as title (link)

Further reading

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This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Gallidermin Provide feedback

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006079

Lantibiotics are heavily-modified bacteriocin-like peptides from Gram-positive bacteria. They contain alpha,beta-unsaturated amino acids (dehydroalanine and dehydrobutyrine) and lanthionine or 3-methyllanthionine rings (collectively known as thioether rings). There are 2 types of lantibiotic:

  • Type A (which include nisin, subtilin, epidermin, gallidermin and Pep5) are strongly cationic and bactericidal - nisin, subtilin and Pep5 inhibit the growth of Gram-positive bacteria, probably by voltage-dependent pore formation in the cytoplasmic membrane, resulting in cellular efflux of electrolytes, amino acids and ATP;
  • Type B lantibiotics possess at most one positive charge and are not bactericidal.

This entry represents type A Lantibiotics that are mostly from Bacillales.

Gene Ontology

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Seed source: IPR001049
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Mian N , Bateman A
Number in seed: 3
Number in full: 27
Average length of the domain: 45.10 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 78.16 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.2 20.2
Trusted cut-off 20.2 21.0
Noise cut-off 19.7 18.9
Model length: 52
Family (HMM) version: 16
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Gallidermin domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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