Protein Family Models

This family includes bacterial extracellular solute-binding proteins. (from Pfam)

Date:

2024-08-14

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)

Date:

2024-10-16

Gene:

wtpA

Date:

2020-10-26

Members of this protein family are tungstate (and, more weakly, molybdate) binding proteins of tungstate(/molybdate) ABC transporters, as first characterized in Pyrococcus furiosus. Model seed members and cutoffs, pending experimental evidence for more distant homologs, were chosen such that this model identifies select archaeal proteins, excluding weaker archaeal and all bacterial homologs. Note that this family is homologous to molybdate transporters, and that at least one other family of tungstate transporter binding protein, TupA, also exists.

Gene:

wtpA

Date:

2024-05-30

molybdate/tungstate ABC transporter substrate-binding protein WtpA is part of the ABC transporter complex WtpABC that is involved in molybdate/tungstate import

Date:

2019-10-04