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ABC transporter substrate-binding protein
This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport [1,2,3]. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043). [1]. 2651410. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. Staudenmaier H, Van Hove B, Yaraghi Z, Braun V;. J Bacteriol 1989;171:2626-2633. [2]. 12475936. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Borths EL, Locher KP, Lee AT, Rees DC;. Proc Natl Acad Sci U S A. 2002;99:16642-16647. [3]. 14514690. The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport. Sebulsky MT, Shilton BH, Speziali CD, Heinrichs DE;. J Biol Chem. 2003;278:49890-49900. (from Pfam)
siderophore ABC transporter substrate-binding protein
siderophore ABC transporter substrate-binding protein such as Bacillus subtilis petrobactin-binding protein YclQ, which is part of the ABC transporter complex YclNOPQ involved in uptake of ferric-petrobactin, a photoreactive 3,4-catecholate siderophore, and which selectively binds iron-free and ferric petrobactin and the petrobactin precursor 3,4-dihydroxybenzoic acid
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