Extended Data Fig. 9: Diverse functional amyloid systems identified from across bacteria.

(a) Operonic and architectural organization of related components of selected Curli and Fap-like systems. A key shows the predicted functions/features annotated by color and outline: blue, transcription factor; purple, amyloid; yellow, peptidase; green, accessory protein; red, amyloid inhibitor; grey, other and/or lineage specific proteins. The presence of a signal peptide within the protein is indicated by an outline. Accession numbers correspond to the protein denoted with an asterisk. Operons found within phage are denoted with a box. (b) Protein domains identified within Curli and Fap-like systems grouped based on their predicted function. Colors correspond to (a). RGG, Arginine-Glycine-Glycine motif characteristic of these proteins; CD-iREC, inactive receiver domain; REC, receiver domain; HTH, helix-turn-helix domain; PAS, Per-Arnt-Sim domain; SSB, single strand DNA binding domain; β-sand, β-sandwich domain; PGBD, peptidoglycan bindings domain; IG, immunoglobulin. (c) Select protein structures from Curli and Fap-like systems that share homology with each other: the iREC (inactive receiver) domain of CsgD and REC (receiver) domain of VspR, the major transcriptional factors that regulate their respective system; CsgA and FapC, the major amyloid subunits of each system. CsgF and FapA, CsgF is known to contribute to secretion across the outer membrane; however, the role of FapA is still unclear. CsgG and FapF are the outer membrane transporters for each system. Protein structures are predicted using AlphaFold2 unless otherwise indicated.