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ATP-binding cassette domain-containing protein
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)
xylose ABC transporter ATP-binding protein
xylose ABC transporter ATP-binding protein (XylG) is the ATPase catalytic subunit of the ABC transporter complex XylFGH, and is responsible for coupling the energy of ATP hydrolysis to the import of xylose
D-xylose ABC transporter ATP-binding protein
Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (PF00005).
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