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1.C.30 The Plantaricin JK (Plantaricin JK) Family

Many organisms synthesize proteins (or peptides) which are degraded to relatively small hydrophobic or amphipathic, bioactive peptides. These peptides exhibit antibiotic, fungicidal, virucidal, hemolytic and/or tumoricidal activities by interacting with membranes and forming transmembrane channels that allow the free flow of electrolytes, metabolites and water across the phospholipid bilayers. Most of these peptides appear to function in biological warfare. There are many designations given to these bioactive peptides. They include the magainins, cecropins, melittins, defensins, bacteriocidins, etc. The proteins in each family within this functional superfamily are homologous, but they exhibit little or no significant sequence similarity with members of the other families. Thus, each family may have evolved independently. However, certain common structural features observed between members of distinct families suggest that at least some of these families share a common ancestry.

The generalized transport reaction catalyzed by channel-forming amphipathic peptides is:

small solutes, electrolytes and water (in) small solutes, electrolytes and water (out).

Bacteriocins are bacterially produced peptide antibiotics with the ability to kill a limited range of bacteria, usually but not always those that are closely related to the producer bacterium. Many of them exhibit structural features typical of members of the eukaryotic channel-forming amphipathic peptides. That is, they are usually synthesized as small precursor proteins or peptides which are processed with proteolytic elimination of their N-terminal leader sequences, and the resultant mature peptides form one, two or more putative amphipathic transmembrane α-helical spanners (TMSs). For those with two TMSs, a characteristic hinge region that separates the two putative transmembrane segments is usually observed. A similar structural arrangement occurs in the two-TMS Cecropin A proteins (TC #1.C.17).

Many bacteriocins are encoded in operons that also encode an immunity protein and an ABC transport system (TC #3.A.1) with a protease domain at the N-terminus. The ABC systems export the bacteriocins while the protease domains cleave the N-terminal leader sequence. A few bacteriocins are exported by the type II general secretory pathway rather than by ABC-type export systems. In some cases, expression of the bacteriocin-encoding operon is induced by a bacteriocin-like peptide which acts in conjunction with a two component sensor kinase-response regulator to effect induction.

IIb, Poration complexes requiring two peptides for activity.

Many bacteriocins have been identified in addition to those tabulated in the TC system, but those listed are among the best characterized, with respect to evidence for channel formation in target bacterial membranes. Class III and IV bacteriocins (Klaenhammer, 1993) are large heat-labile proteins that function by mechanisms unrelated to those of the bacteriocins listed here.

This family belongs to the: Bacterial Bacteriocin (BB) Superfamily.

References associated with 1.C.30 family:

Ahn S.J., R.A. Burne. (2006). The atlA operon of Streptococcus mutans: role in autolysin maturation and cell surface biogenesis. J. Bacteriol. 188: 6877-6888. 16980491
Allison, G.E., C. Fremaux and T.R. Klaenhammer (1994). Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J. Bacteriol. 176: 2235-2241. 8157592
Diep, D.B., L.S. Håvarstein and I.F. Nes (1995). A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11. Mol. Microbiol. 18: 631-639. 8817486
Klaenhammer, T.R. (1993). Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 12: 39-85. 8398217
Moll, G.N., E. van den Akker, H.H. Hauge, J. Nissen-Meyer, I.F. Nes, W.N. Konings and A.J.M. Driessen (1999). Complementary and overlapping selectivity of the two-peptide bacteriocins plantaricin EF and JK. J. Bacteriol. 181: 4848-4852. 10438754
Moll, G.N., W.N. Konings and A.J.M. Driessen (1999). Bacteriocins: mechanism of membrane insertion and pore formation. Antonie van Leeuwenhoek 76: 185-198. 10532378
Nes, I.F., D.B. Diep, L.S. Håvarstein, M.B. Brurberg, V. Eijsink and H. Holo (1996). Biosynthesis of bacteriocins in lactic acid bacteria. Antonie van Leeuwenhoek 70: 113-128. 8879403
Oppegård, C., P. Rogne, L. Emanuelsen, P.E. Kristiansen, G. Fimland, and J. Nissen-Meyer. (2007). The two-peptide class II bacteriocins: structure, production, and mode of action. J. Mol. Microbiol. Biotechnol. 13: 210-219. 17827971
Sahl, H.-G. and G. Bierbaum (1998). Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria. Annu. Rev. Microbiol. 52: 41-79. 9891793
Sharma, A. and S. Srivastava. (2014). Anti-Candida activity of two-peptide bacteriocins, plantaricins (Pln E/F and J/K) and their mode of action. Fungal Biol 118: 264-275. 24528647
Venema, K., G. Venema and J. Kok (1995). Lactococcal bacteriocins: mode of action and immunity. Trends Microbiol. 3: 299-304. 8528613