Probably 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). Does not form amyloid fibrils in vitro, unlike RdlB (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 aerial hyphae and spores (at protein level). During aerial hyphae formation. The N-terminus of RdlA is more highly charged than the same region in RdlB; replacing 3 charged residues by polar residues confers the ability to form amyloid rods to RdlA and allows the mutant protein to form rodlets by itself, which neither RdlA or RdlB can do alone. A single rdlA mutant does not form the rodlet layer on spore cell walls; disruption can be complemented by rdlA from S.tendae or S.griseus but not by any rdlB. Decreased levels of rdlB 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.