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extracellular solute-binding protein
This family includes bacterial extracellular solute-binding proteins. (from Pfam)
DUF3502 domain-containing protein
This presumed domain is functionally uncharacterised. This domain is found in bacteria. This domain is about 140 amino acids in length. This domain is found associated with Pfam:PF01547. [1]. 28045395. Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092. Culurgioni S, Tang M, Walsh MA;. Acta Crystallogr F Struct Biol Commun. 2017;73:54-61. (from Pfam)
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)
ABC transporter substrate-binding protein
ABC transporter substrate-binding protein is a type 2 periplasmic binding protein (PBP2) that functions as the initial receptor in the ABC transport of one or more from a variety of substrates such as carbohydrates; contains a DUF3502 domain
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