Bacteriocin hiracin-JM79
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Bacteriocin hiracin-JM79

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Bacteriocin hiracin-JM79 is an antimicrobial peptide found in Enterococcus hirae DCH5. It has antibacterial activity against the Gram-positive bacteria: Listeria, Enterococcus, Propionibacterim, Staphylococcus and some strains of Clostridium, Lactobacillus and Pediococcus, and no antibacterial activity against Gram-negative bacteria.

Functional Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
HirJM79 (Bacteriocin); Hiracin-JM79 (Bacteriocin); Ala-Thr-Tyr-Tyr-Gly-Asn-Gly-Leu-Tyr-Cys-Asn-Lys-Glu-Lys-Cys-Trp-Val-Asp-Trp-Asn-Gln-Ala-Lys-Gly-Glu-Ile-Gly-Lys-Ile-Ile-Val-Asn-Gly-Trp-Val-Asn-His-Gly-Pro-Trp-Ala-Pro-Arg-Arg
Lyophilized Powder or Liquid
Store at -20°C
1. Cloning and heterologous production of Hiracin JM79, a Sec-dependent bacteriocin produced by Enterococcus hirae DCH5, in lactic acid bacteria and Pichia pastoris
Jorge Sánchez, Juan Borrero, Beatriz Gómez-Sala, Antonio Basanta, Carmen Herranz, Luis M Cintas, Pablo E Hernández Appl Environ Microbiol. 2008 Apr;74(8):2471-9. doi: 10.1128/AEM.02559-07. Epub 2008 Feb 29.
Hiracin JM79 (HirJM79), a Sec-dependent bacteriocin produced by Enterococcus hirae DCH5, was cloned and produced in Lactococcus lactis, Lactobacillus sakei, Enterococcus faecium, Enterococcus faecalis, and Pichia pastoris. For heterologous production of HirJM79 in lactic acid bacteria (LAB), the HirJM79 structural gene (hirJM79), with or without the HirJM79 immunity gene (hiriJM79), was cloned into the plasmid pMG36c under the control of the constitutive promoter P(32) and into the plasmid pNZ8048 under the control of the inducible P(NisA) promoter. For the production of HirJM79 in P. pastoris, the gene encoding the mature HirJM79 protein was cloned into the pPICZalphaA expression vector. The recombinant plasmids permitted the production of biologically active HirJM79 in the supernatants of L. lactis IL1403, L. lactis NZ9000, L. sakei Lb790, E. faecalis JH2-2, and P. pastoris X-33, the coproduction of HirJM79 and nisin A in L. lactis DPC5598, and the coproduction of HirJM79 and enterocin P in E. faecium L50/14-2. All recombinant LAB produced larger quantities of HirJM79 than E. hirae DCH5, although the antimicrobial activities of most transformants were lower than that predicted from their production of HirJM79. The synthesis, processing, and secretion of HirJM79 proceed efficiently in recombinant LAB strains and P. pastoris.
2. Amino acid and nucleotide sequence, adjacent genes, and heterologous expression of hiracin JM79, a sec-dependent bacteriocin produced by Enterococcus hirae DCH5, isolated from Mallard ducks (Anas platyrhynchos)
Jorge Sánchez, Dzung B Diep, Carmen Herranz, Ingolf F Nes, Luis M Cintas, Pablo E Hernández FEMS Microbiol Lett. 2007 May;270(2):227-36. doi: 10.1111/j.1574-6968.2007.00673.x. Epub 2007 Feb 26.
The primary structure of a bacteriocin produced by Enterococcus hirae DCH5 was determined by combined amino acid and DNA sequencing. Nucleotide analysis of a 2838-bp DNA fragment of E. hirae DCH5 revealed five putative ORFs. The first orf (hirJM79) encodes a 74-amino-acid peptide containing an N-terminal signal peptide of 30 amino acids, followed by the amino acid sequence of the mature bacteriocin, hiracin JM79 (HirJM79), of 44 amino acids. The second orf (hiriJM79) encodes the putative immunity protein of HirJM79. Contiguous ORFs encode a putative mobilization protein (orfC), a relaxase/mobilization nuclease domain (orfD), and a hypothetical protein (orfE). The production and functional expression of HirJM79 by heterologous hosts suggest that hirJM79 is the minimum requirement for production of biologically active HirJM79, that HirJM79 is most likely externalized by the general secretory pathway or sec-dependent pathway, and that HiriJM79 is the immunity protein for HirJM79.
3. Modified lactic acid bacteria detect and inhibit multiresistant enterococci
Juan Borrero, Yuqing Chen, Gary M Dunny, Yiannis N Kaznessis ACS Synth Biol. 2015 Mar 20;4(3):299-306. doi: 10.1021/sb500090b. Epub 2014 Jun 16.
We designed Lactococcus lactis to detect Enterococcus faecalis. Upon detection, L. lactis produce and secrete antienterococcal peptides. The peptides inhibit enterococcal growth and reduce viability of enterococci in the vicinity of L. lactis. The enterococcal sex pheromone cCF10 serves as the signal for detection. Expression vectors derived from pCF10, a cCF10-responsive E. faecalis sex-pheromone conjugative plasmid, were engineered in L. lactis for the detection system. Recombinant host strains were engineered to express genes for three bacteriocins, enterocin A, hiracin JM79 and enterocin P, each with potent antimicrobial activity against E. faecalis. Sensitive detection and specific inhibition occur both in agar and liquid media. The engineered L. lactis also inhibited growth of multidrug-resistant E. faecium strains, when induced by cCF10. The presented vectors and strains can be components of a toolbox for the development of alternative antibiotic technologies targeting enterococci at the site of infection.
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