Protein Family Models

This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with Pfam:PF00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter [1]. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains [2]. [1]. 2195019. Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli. Adams MD, Wagner LM, Graddis TJ, Landick R, Antonucci TK, Gibson AL, Oxender DL;. J Biol Chem 1990;265:11436-11443. [2]. 31431556. Combining Mutations That Inhibit Two Distinct Steps of the ATP Hydrolysis Cycle Restores Wild-Type Function in the Lipopolysaccharide Transporter and Shows that ATP Binding Triggers Transport. Simpson BW, Pahil KS, Owens TW, Lundstedt EA, Davis RM, Kahne D, Ruiz N;. mBio. 2019; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

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

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivG is the ATPase subunit of the complex responsible for coupling the energy of ATP hydrolysis to the import of the hydrophobic amino acids leucine, isoleucine, and valine

Date:

2023-02-27

Part of the ABC transporter complexes LivFGHMJ and LivFGHMK involved in the high-affinity transport of branched-chain amino acids; LivFGHMK is specific for the transport of leucine, while LivFGHMJ is a transporter for leucine, isoleucine, and valine

Gene:

livG

Date:

2021-10-04