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KUP/HAK/KT family potassium transporter
This is a family of K+ potassium transporters that are conserved across phyla, having both bacterial (KUP) Swiss:P30016 [3], yeast (HAK) Swiss:P50505 [2], and plant (AtKT) Swiss:O22397 [1] sequences as members. This entry represents the C-terminal non-membrane domain. [1]. 9350997. A new family of K+ transporters from Arabidopsis that are conserved across phyla. Quintero FJ, Blatt MR;. FEBS Lett 1997;415:206-211. [2]. 7621817. A potassium transporter of the yeast Schwanniomyces occidentalis homologous to the Kup system of Escherichia coli has a high concentrative capacity. Banuelos MA, Klein RD, Alexander-Bowman SJ, Rodriguez-Navarro A;. EMBO J 1995;14:3021-3027. [3]. 8226635. Nucleotide sequence and 3'-end deletion studies indicate that the K(+)-uptake protein kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus. Schleyer M, Bakker EP;. J Bacteriol 1993;175:6925-6931. (from Pfam)
This is a family of K+ potassium transporters that are conserved across phyla, having both bacterial (KUP) Swiss:P30016 [3], yeast (HAK) Swiss:P50505 [2], and plant (AtKT) Swiss:O22397 [1] sequences as members. This entry represents the N-terminal integral membrane domain. [1]. 9350997. A new family of K+ transporters from Arabidopsis that are conserved across phyla. Quintero FJ, Blatt MR;. FEBS Lett 1997;415:206-211. [2]. 7621817. A potassium transporter of the yeast Schwanniomyces occidentalis homologous to the Kup system of Escherichia coli has a high concentrative capacity. Banuelos MA, Klein RD, Alexander-Bowman SJ, Rodriguez-Navarro A;. EMBO J 1995;14:3021-3027. [3]. 8226635. Nucleotide sequence and 3'-end deletion studies indicate that the K(+)-uptake protein kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus. Schleyer M, Bakker EP;. J Bacteriol 1993;175:6925-6931. (from Pfam)
low affinity potassium transporter Kup
potassium transporter Kup is involved in low-affinity potassium ion uptake, probably via coupling to proton influx (symport), under hyper-osmotic stress at a low pH
potassium uptake protein
Proteins of the KUP family include the KUP (TrkD) protein of E. coli, a partially sequenced ORF from Lactococcus lactis, high affinity K+ uptake systems (Hak1) of the yeast Debaryomyces occidentalis as well as the fungus, Neurospora crassa, and several homologues in plants. While the E. coli KUP protein is assumed to be a secondary transporter, and uptake is blocked by protonophores such as CCCP (but not arsenate), the energy coupling mechanism has not been defined. However, the N. crassa protein has been shown to be a K+:H+ symporter, establishing that the KUP family consists of secondary carriers. The plant high affinity (20mM) K+ transporter can complement K+ uptake defects in E. coli.
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