| Description | This entry represents several repeats of the filamentous hemagglutinin (FHA-1) motif, which have approximately 20 amino acids. The repeats are found at the N-terminal domain of Toxin CdiA from Escherichia coli and similar proteins mostly from bacterial species, including several plant and animal pathogens. The FHA-1 repeats found in the extracellular filament of CdiA form an elongated β-helix, with each ~20-residue motif extending the helix [, ].CdiA is a toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighbouring bacteria in a contact-dependent fashion. CDI is neutralised by its cognate immunity protein CdiI, but not by non-cognate CdiI from other bacteria [ , ].Some proteins with nuclease activity on top of the toxin activity are also included in this group, such as tRNA nuclease CdiA from Escherichia coli. This protein cleaves tRNA (CUG-Gln) in the acceptor stem between C70 and A71 [ . 16S rRNA endonuclease CdiA from Enterobacter cloacae cleaves 16S rRNA in vivo and in vitro between adenine 1493 and guanosine 1494 of E.coli 16S rRNA [ ]. | Name | Toxin CdiA-like, Filamentous hemagglutinin motif repeats |
| Short Name | CdiA_FHA1_rpt | Type | Repeat |
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