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TOBE domain-containing protein
The TOBE domain [1] (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum (eg Swiss:P46930) and sulphate (Swiss:P16676). Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain. [1]. 10829230. Protein fold recognition using sequence profiles and its. application in structural genomics.. Koonin EV, Wolf YI, Aravind L;. Adv Protein Chem 2000;54:245-275. (from Pfam)
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)
putative 2-aminoethylphosphonate ABC transporter ATP-binding protein
This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely.
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