Protein Family Models

ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains. [1]. 1864505. Homology between proteins controlling Streptomyces fradiae tylosin resistance and ATP-binding transport. Rosteck PR Jr, Reynolds PA, Hershberger CL;. Gene 1991;102:27-32. [2]. 1977073. Structure and function of haemolysin B,P-glycoprotein and other members of a novel family of membrane translocators. Blight MA, Holland IB;. Mol Microbiol 1990;4:873-880. [3]. 2229036. Binding protein-dependent transport systems. Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP;. J Bioenerg Biomembr 1990;22:571-592. [4]. 9872322. Crystal structure of the ATP-binding subunit of an ABC transporter. Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH;. Nature 1998;396:703-707. (from Pfam)

Date:

2024-10-16

CBS domains are small intracellular modules that pair together to form a stable globular domain [2]. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain [6]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [5]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet [4]. CBS domain pairs from AMPK bind AMP or ATP [5]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [5]. Discovery and naming of the CBS domain. [1]. 9020585. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Bateman A;. Trends Biochem Sci 1997;22:12-13. 3D Structure found as a sub-domain in TIM barrel of inosine-monophosphate dehydrogenase. [2]. 10200156. Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR;. Biochemistry 1999;38:4691-4700. Discovery of CBS domain. [3]. 9106071. CBS domains in ClC chloride channels implicated in myotonia and nephrolithiasis (kidney stones). Ponting CP;. J Mol Med 1997;75:160-163. [4]. 11524006. Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. Janosik M, Kery V, Gaustadnes M, Macl. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

With ProWX is involved in the high-affinity uptake of glycine betaine

Gene:

proV

Date:

2021-08-30

This model describes the ATP binding subunit of a subfamily of ABC transporters, including ProV (for glycine betaine and proline betaine transport), OpuBA (choline), OpuCA (carnitine), GbuA (glycine betaine and carnitine), OusV (glycine betaine and choline), etc. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system includes an ATP binding (and hydrolyzing) subunit; a hydrophilic polypeptide that forms a channel through the membrane, and a substrate binding protein; any of these subunits may be represented by two paralogs instead of just one. Substrates for many members of this transport system, such as glycine betaine (a glycine with its N trimethylated, often simply called betaine), serve as osmoprotectants , although they also may serve as nutrients.

Date:

2024-06-14