Protein Family Models

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

Date:

2024-08-14

Part of a high affinity multicomponent binding-protein-dependent transport system involved in bacterial osmoregulation. This domain is often fused to the permease component of the transporter complex. Family members are often integral membrane proteins or predicted to be attached to the membrane by a lipid anchor. Glycine betaine is involved in protection from high osmolarity environments for example in Bacillus subtilis [1]. The family member OpuBC is closely related, and involved in choline transport. Choline is necessary for the biosynthesis of glycine betaine [2]. L-carnitine is important for osmoregulation in Listeria monocytogenes. Family also contains proteins binding l-proline (ProX), histidine (HisX) and taurine (TauA). [1]. 7622480. OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. Kempf B, Bremer E;. J Biol Chem 1995;270:16701-16713. [2]. 10216873. Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis. Kappes RM, Kempf B, Kneip S, Boch J, Gade J, Meier-Wagner J, Bremer E;. Mol Microbiol 1999;32:203-216. [3]. 11055912. Identification and characterization of an ATP binding cassette L-carnitine transporter in Listeria monocytogenes. Fraser KR, Harvie D, Coote PJ, O'Byrne CP;. Appl Environ Microbiol 2000;66:4696-4704. (from Pfam)

Date:

2024-10-16

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

molybdate ABC transporter substrate-binding protein srves as the initial receptor in the ABC transport of molybdate; similar to Haemophilus influenzae putative binding protein HI_1525

Date:

2023-10-03

The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains.

Gene:

modA

Date:

2024-07-12