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They have a modular organization comprising a receptor\u2010binding domain recognizing a surface constituent of the target bacterium, a domain for translocation through the periplasm, and a killing or toxic domain with <jats:styled-content style=\"fixed-case\">DN<\/jats:styled-content>ase, <jats:styled-content style=\"fixed-case\">tRN<\/jats:styled-content>ase, or pore\u2010forming activity. Pyocins S2, S3, S4, and S5 recognize TonB\u2010dependent ferri\u2010siderophore receptors in the outer membrane. We here describe a new nuclease bacteriocin, pyocin S6, encoded in the genome of a <jats:italic>P. aeruginosa<\/jats:italic> cystic fibrosis (<jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content>) clinical isolate, <jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content>_<jats:styled-content style=\"fixed-case\">PA<\/jats:styled-content>39. Similarly to pyocins S1 and S2, the S6 toxin\u2013immunity gene tandem was recruited to the genomic region encoding exotoxin A. The pyocin S6 receptor\u2010binding and translocation domains are identical to those of pyocin S1, whereas the killing domain is similar to the 16S ribonuclease domain of <jats:italic>Escherichia coli<\/jats:italic> colicin E3. The cytotoxic activity was abolished in pyocin S6 forms with a mutation in the colicin E3\u2010equivalent catalytic motif. The <jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content>_<jats:styled-content style=\"fixed-case\">PA<\/jats:styled-content>39 S6 immunity gene displays a higher expression level than the gene encoding the killing protein, the latter being only detected when bacteria are grown under iron\u2010limiting conditions. In the S1\u2010pyocinogenic strain <jats:italic>P. aeruginosa <\/jats:italic><jats:styled-content style=\"fixed-case\">ATCC<\/jats:styled-content> 25324 and pyocin S2 producer <jats:italic>P. aeruginosa <\/jats:italic><jats:styled-content style=\"fixed-case\">PAO<\/jats:styled-content>1, a remnant of the pyocin S6 killing domain and an intact S6\u2010type immunity gene are located downstream of their respective pyocin operons. Strain <jats:styled-content style=\"fixed-case\">PAO<\/jats:styled-content>1 is insensitive for pyocin S6, and its S6\u2010type immunity gene provides protection against pyocin S6 activity. Purified pyocin S6 inhibits one\u2010fifth of 110 <jats:italic>P. aeruginosa <\/jats:italic><jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content> clinical isolates tested, showing clearer inhibition zones when the target cells are grown under iron limitation. In this panel, about half of the <jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content> clinical isolates were found to host the S6 genes. The pyocin S6 locus is also present in the genome of some non\u2010<jats:styled-content style=\"fixed-case\">CF<\/jats:styled-content> clinical isolates.<\/jats:p>","DOI":"10.1002\/mbo3.339","type":"journal-article","created":{"date-parts":[[2016,2,10]],"date-time":"2016-02-10T07:07:14Z","timestamp":1455088034000},"page":"413-423","source":"Crossref","is-referenced-by-count":38,"title":["Identification and functional analysis of a bacteriocin, pyocin S6, with ribonuclease activity from a <i>Pseudomonas aeruginosa<\/i> cystic fibrosis clinical isolate"],"prefix":"10.1002","volume":"5","author":[{"given":"Jozef","family":"Dingemans","sequence":"first","affiliation":[{"name":"Department of Bioengineering Sciences Research group Microbiology and VIB Department of Structural Biology Vrije Universiteit Brussel  Pleinlaan 2 Brussels 1050 Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maarten G. 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