Forms part of the rodlet layer on the spore surface; despite their high similarity both RdlA and RdlB are required for rodlet formation (PubMed:12067338, PubMed:15228525). Plays a role in cell adhesion to polystyrene plates (PubMed:12067338). Forms amyloid-like fibrils in vitro composed of stacked beta-sheets (PubMed:28211492). Found on the surface of aerial hyphae and probably on the surface of the spore wall (PubMed:12067338). Rodlins probably contribute to the semi-transparent sheath-like structure which encapsulates spores, probably outside the chaplin layer (Probable). Present in aerial but not submerged hyphae, persists as hyphae differentitate and form spores; present at the outer surface of these structures (at protein level). During aerial hyphae formation. The mature protein has 2 regions in the N-terminus capable of forming amyloid rods of slightly differing conformation; intact protein makes longer fibrils. Amyloid formation depends on polar residues between amino acids 45 and 70. A single rdlB mutant does not form the rodlet layer on spores; disruption can be complemented by rdlB from S.tendae or S.griseus but not by any rdlA. Decreased levels of rdlA mRNA (PubMed:15228525). A double rdlA-rdlB deletion shows no effect on spore germination, growth rates, differentiation of aerial hyphae into spores or surface hydrophobicity on a number of media, but spore surface rodlets are missing and cells adhere less strongly to a polysytrene surface (PubMed:12067338). In the double rdlA-rdlB mutant chaplin proteins are still correctly localized to the cell wall of aerial hyphae (PubMed:12832396). In the double rdlA-rdlB mutant aerial hyphae development is strongly delayed under high osmolarity (10.3% sucrose or 0.5 M KCl) (PubMed:22309453). Belongs to the rodlin family.