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Lectin\u2010like bacteriocins are atypical bacteriocins not requiring a cognate immunity factor and have been primarily studied in\n                    <jats:italic>Pseudomonas<\/jats:italic>\n                    . These so\u2010called LlpAs are composed of a tandem of B\u2010lectin domains. One domain interacts with\n                    <jats:sc>d<\/jats:sc>\n                    \u2010rhamnose residues in the common polysaccharide antigen of\n                    <jats:italic>Pseudomonas<\/jats:italic>\n                    lipopolysaccharide (\n                    <jats:styled-content style=\"fixed-case\">LPS<\/jats:styled-content>\n                    ). The other lectin domain is crucial for interference with the outer membrane protein assembly machinery by interacting with surface\u2010exposed loops of its central component BamA. Via genome mining, we identified a second subclass of\n                    <jats:italic>Pseudomonas<\/jats:italic>\n                    lectin\u2010like proteins, termed LlpB, consisting of a single B\u2010lectin domain. We show that these proteins also display bactericidal activity. Among LlpB\u2010resistant transposon mutants of an LlpB\u2010susceptible\n                    <jats:italic>Pseudomona<\/jats:italic>\n                    s strain, a major subset was hit in an acyltransferase gene, predicted to be involved in\n                    <jats:styled-content style=\"fixed-case\">LPS<\/jats:styled-content>\n                    core modification, hereby suggesting that LlpBs equally attach to\n                    <jats:styled-content style=\"fixed-case\">LPS<\/jats:styled-content>\n                    for surface anchoring. This indicates that\n                    <jats:styled-content style=\"fixed-case\">LPS<\/jats:styled-content>\n                    binding and target strain specificity are condensed in a single B\u2010lectin domain. The identification of this second subclass of lectin\u2010like bacteriocins further expands the toolbox of antibacterial warfare deployed by bacteria and holds potential for their integration in biotechnological applications.\n                  <\/jats:p>","DOI":"10.1111\/1751-7915.13373","type":"journal-article","created":{"date-parts":[[2019,1,31]],"date-time":"2019-01-31T08:16:57Z","timestamp":1548922617000},"page":"567-573","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["LlpB represents a second subclass of lectin\u2010like bacteriocins"],"prefix":"10.1111","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5577-7277","authenticated-orcid":false,"given":"Maarten G. 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