cd02078

potassium-transporting ATPase ATP-binding subunit, KdpB, a subunit of the prokaryotic high-affinity potassium uptake system KdpFABC; similar to Escherichia coli KdpB

CDD entry
Member databaseCDD
CDD typedomain
Short nameP-type_ATPase_K
SetHAD_like

Description

KdpFABC is a prokaryotic high-affinity potassium uptake system. It is expressed under K(+) limiting conditions when the other potassium transport systems are not able to provide a sufficient flow of K(+) into the bacteria. The KdpB subunit represents the catalytic subunit performing ATP hydrolysis. KdpB is comprised of four domains: the transmembrane domain, the nucleotide-binding domain, the phosphorylation domain, and the actuator domain. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.
[16, 2, 15, 6, 1, 11, 9, 13, 8, 10, 7, 4, 14, 3, 5, 12]

References

1.New type of kdp region with a split sensor-kinase kdpD gene located within two divergent kdp operons from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius. Schleussinger E, Schmid R, Bakker EP. Biochim Biophys Acta 1759, 437-41, (2006). PMID: 17023259

2.The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone. Irzik K, Pfrotzschner J, Goss T, Ahnert F, Haupt M, Greie JC. FEBS J 278, 3041-53, (2011). PMID: 21711450

3.The p-type ATPase superfamily. Chan H, Babayan V, Blyumin E, Gandhi C, Hak K, Harake D, Kumar K, Lee P, Li TT, Liu HY, Lo TC, Meyer CJ, Stanford S, Zamora KS, Saier MH Jr. J Mol Microbiol Biotechnol 19, 5-104, (2010). PMID: 20962537

4.The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Aravind L, Galperin MY, Koonin EV. Trends Biochem. Sci. 23, 127-9, (1998). View articlePMID: 9584613

5.P-type ATPases. Palmgren MG, Nissen P. Annu Rev Biophys 40, 243-66, (2011). PMID: 21351879

6.Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase. Damnjanovic B, Weber A, Potschies M, Greie JC, Apell HJ. Biochemistry 52, 5563-76, (2013). PMID: 23930894

7.Evolution of P-type ATPases. Palmgren MG, Axelsen KB. Biochim. Biophys. Acta 1365, 37-45, (1998). View articlePMID: 9693719

8.How do P-type ATPases transport ions? Apell HJ. Bioelectrochemistry 63, 149-56, (2004). PMID: 15110265

9.Sequence homology between two membrane transport ATPases, the Kdp-ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum. Hesse JE, Wieczorek L, Altendorf K, Reicin AS, Dorus E, Epstein W. Proc Natl Acad Sci U S A 81, 4746-50, (1984). PMID: 6146979

10.Rethinking the P-type ATPase problem. Scarborough GA. Trends Biochem Sci 28, 581-4, (2003). PMID: 14607087

11.The kdp system of Clostridium acetobutylicum: cloning, sequencing, and transcriptional regulation in response to potassium concentration. Treuner-Lange A, Kuhn A, Durre P. J. Bacteriol. 179, 4501-12, (1997). View articlePMID: 9226259

12.P-type ATPases at a glance. Bublitz M, Morth JP, Nissen P. J Cell Sci 124, 2515-9, (2011). PMID: 21768325

13.The roles and regulation of potassium in bacteria. Epstein W. Prog Nucleic Acid Res Mol Biol 75, 293-320, (2003). PMID: 14604015

14.Biology, structure and mechanism of P-type ATPases. Kuhlbrandt W. Nat Rev Mol Cell Biol 5, 282-95, (2004). PMID: 15071553

15.The holo-form of the nucleotide binding domain of the KdpFABC complex from Escherichia coli reveals a new binding mode. Haupt M, Bramkamp M, Heller M, Coles M, Deckers-Hebestreit G, Herkenhoff-Hesselmann B, Altendorf K, Kessler H. J. Biol. Chem. 281, 9641-9, (2006). View articlePMID: 16354672

16.Absolute quantification of the Kdp subunits of Escherichia coli by multiple reaction monitoring. Surmann K, Laermann V, Zimmann P, Altendorf K, Hammer E. Proteomics 14, 1630-8, (2014). PMID: 24829208

Integrated to
External Links
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.