Table 1.
Selected microbial RiPPs covering different chemical classes cited in this review for which an ecological function has been described
| RiPP class | RiPP name | Producing strains (examples) | Ecological role | Mode of antibacterial action (when applicable) | References |
|---|---|---|---|---|---|
| Circular bacteriocin | Enterocin AS-48/Bac-21 | E. faecalis AS-48, OG1RF | Interference competition | Pore-forming activity | 68 |
| Cyclic peptide | AIP | S. aureus, S. hominis | Quorum-sensing signala | 137, 152, 154 | |
| Cyclic peptide | Streptide | S. thermophilus | Quorum-sensing responseb | 175–177 | |
| Lanthipeptide (lantibiotic) | Nisinc | L. lactis | Autoinducing peptidea | Pore-forming activity; Blocking of peptidoglycan synthesis (binding to lipid II) | 83–86, 88 |
| Lanthipeptide (two-peptide lantibiotic) | Sh-lantibiotics-α/β | S. hominis A9 | Interference competition | Unknown | 135 |
| Lanthipeptide | SapB/SapT | S. coelicolor, S. tendae | Morphological development in Streptomyces | 194, 195 | |
| Lanthipeptide (lantibiotic) | Planosporicinc | Planomonospora alba | Autoinducing peptidea | Blocking of peptidoglycan biosynthesis (binding to lipid II) | 167, 238 |
| Lanthipeptide (lantibiotic) | Unnamed | S. pneumoniae | Quorum-sensing response; niche competition | Unknown | 170 |
| Lanthipeptide (two-peptide lantibiotics) | Cytolysin | E. faecalis | Autoinducing peptidea; virulence factor | Pore-forming activity | 169 |
| Lanthipeptide (two-peptide lantibiotics) | Lacticin 3147 (LtnA1/LtnA2) | L. lactis | Interference competition | Pore-forming activity (LtnA1/LtnA2/lipid II synergy) | 133, 134 |
| Lasso peptide | Microcin J25 | E. coli AY25 | Interference competition | Blocking of transcription (binding to RNA polymerase) | 55, 65 |
| Methanobactin | Methanobactin | Methylosinus trichosporium | Metallophore | 207 | |
| Modified short peptide | ComX | B. subtilis | Quorum-sensing signala | 158 | |
| Modified small peptide | RaxX | X. oryzae pv. oryzae | Host-bacteria interaction | 181 | |
| Peptide-derived small molecule | Pyrroloquinoline quinone | K. pneumoniae | Redox enzyme cofactor | 217 | |
| Peptide-derived small molecule | Mycofactocin | M. tuberculosis | Redox enzyme cofactor | 216, 225 | |
| Sactipeptide | Sporulation killing factor | B. subtilis 168 | Cannibalism | 202 | |
| Sactipeptide (sactibiotic) | Ruminococcin C | R. gnavus E1 | Interference competition | Perturbation of nucleic acid synthesis | 32, 33, 239 |
| Sactipeptide (two-peptide sactibiotic) | Thuricin CD (Trnα/Trnβ) | B. thuringiensis DPC 6431 | Interference competition | Pore-forming activity | 240 |
| Siderophore peptide | Microcin E492/E492m | K. pneumoniae RYC492 E. coli VCS257 with pJAM229 plasmid | Interference competition; exploitative competition (iron) | Pore-forming activity; Perturbation of mannose transport | 44–47 |
| Siderophore peptide | Microcin H47 Microcin M | E. coli H47, Nissle 1917, CA46, CA58 | Interference competition; exploitative competition (iron) | Perturbation of ATP synthesis | 42, 107 |
| Thiopeptide | Lactocillin | L. gasseri | Interference competition | Unknown | 31 |
| Thiopeptide | Thiocillinc | B. cereus | Stimulation of biofilm formation in Bacillus | Inhibition of ribosomal protein synthesis (binding to EF-Tu) | 191 |
| Thiopeptide | Thiostreptonc | S. laurentii | Morphological development in Streptomyces | Inhibition of ribosomal protein synthesis (binding to EF-Tu) | 200 |
| TOMM/LAP | Goadsporinc | Streptomyces sp. | Morphological development in Streptomyces | Unknown | 199 |
| TOMM/LAP | Listeriolysin S | L. monocytogenes | Interference competition (virulence factor) | Unknown | 139–141, 241 |
| TOMM/LAP | Streptolysin S | S. pyogenes | Virulence factor (cytotoxin) | 71 |
a The terms of autoinducing peptide and quorum-sensing signal are distinguished, the former describing peptides that only autoinduce their own production and the latter relating to peptides that also regulate transcription of other genes in addition to autoinduction.
b Other physiological functions have not been identified.
c Also an antibacterial peptide, but its function in niche competition has not yet been demonstrated.