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substrate-binding domain-containing protein
This family includes bacterial extracellular solute-binding proteins. (from Pfam)
ABC transporter substrate-binding protein
extracellular solute-binding protein
This family also includes the bacterial extracellular solute-binding protein family POTD/POTF. [1]. 2002054. The 2.3-A resolution structure of the maltose- or. maltodextrin-binding protein, a primary receptor of bacterial. active transport and chemotaxis.. Spurlino JC, Lu GY, Quiocho FA;. J Biol Chem 1991;266:5202-5219.. [2]. 9360608. Structure of Haemophilus influenzae Fe(+3)-binding protein. reveals convergent evolution within a superfamily.. Bruns CM, Nowalk AJ, Arvai AS, McTigue MA, Vaughan KG, Mietzner. TA, McRee DE;. Nat Struct Biol 1997;4:919-924.. [3]. 9651355. Crystal structure and mutational analysis of the Escherichia. coli putrescine receptor. Structural basis for substrate. specificity.. Vassylyev DG, Tomitori H, Kashiwagi K, Morikawa K, Igarashi K;. J Biol Chem 1998;273:17604-17609.. [4]. 8336670. Structural, functional, and evolutionary relationships among. extracellular solute-binding receptors of bacteria.. Tam R, Saier MH Jr;. Microbiol Rev 1993;57:320-346. (from Pfam)
putative 2-aminoethylphosphonate ABC transporter substrate-binding protein
putative 2-aminoethylphosphonate ABC transporter substrate-binding protein may be part of the PhnSTUV complex (TC 3.A.1.11.5) involved in 2-aminoethylphosphonate import
This ABC transporter extracellular solute-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely.
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