Résumé
Class II microcins are 4.9- to 8.9-kDa polypeptides produced by and active against enterobacteria. They are classified into two subfamilies according to their structure and their gene cluster arrangement. While class IIa microcins undergo no posttranslational modification, class IIb microcins show a conserved C-terminal sequence that carries a salmochelin-like siderophore motif as a posttranslational modification. Aside from this C-terminal end, which is the signature of class IIb microcins, some sequence similarities can be observed within and between class II subclasses, suggesting the existence of common ancestors. Their mechanisms of action are still under investigation, but several class II microcins use inner membrane proteins as cellular targets, and some of them are membrane-active. Like group B colicins, many, if not all, class II microcins are TonB- and energy-dependent and use catecholate siderophore receptors for recognition/translocation across the outer membrane. In that context, class IIb microcins are considered to have developed molecular mimicry to increase their affinity for their outer membrane receptors through their salmochelin-like posttranslational modification.