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InterPro: IPR000695 ATPase, P-type, H+ transporting proton pump

Protein matchesHelp
UniProtKB
Matches:
3833 proteins
AccessionHelp IPR000695 ATPase_P-typ_H-transp
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR001757 ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
Children IPR006413 ATPase, P-type, calcium-transporting, PMR1-type
IPR006415 ATPase, P-type, magnesium-translocating
IPR006534 ATPase, P-type, plasma-membrane proton-efflux
Contains IPR005834 Haloacid dehalogenase-like hydrolase
IPR008250 ATPase, P-type, ATPase-associated domain
GO Term annotationHelp
Process GO:0006754 ATP biosynthetic process
Function GO:0005524 ATP binding
GO:0015662 ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
Component GO:0016020 membrane
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport [1, 2].

  • F-ATPases (F1F0-ATPases) in mitochondria, chloroplasts and bacterial plasma membranes are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles, catalysing ATP hydrolysis to transport solutes and lower pH in organelles.
  • A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.
  • P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

P-ATPases (sometime known as E1-E2 ATPases) (EC:3.6.3.-) are found in bacteria and in a number of eukaryotic plasma membranes and organelles [3]. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, each of which transports a specific type of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+ and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+ and Cu2+. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.

H+-Transporting ATPases (proton pumps) are the main ion pumps in the plasma membrane and play a central role [4] in the physiology and bioenergetics of plant cells. They are the primary active transporters of the plasma membrane and are responsible for generating the membrane potential that drives translocation of cations, amino-acids, sugars, and hormones, whilst also contributing to the maintenance of intracellular and extracellular pH and cell turgor [5]. Proton pumps are members of the P-type (or E1-E2-type) cation-transporting ATPase superfamily, which has evolved from a common ancestral gene [6]. The sequences are believed to contain 8-10 transmembrane helices, some of which are well conserved throughout the superfamily. They may thus all operate via a similar mechanism, with an aspartylphosphoryl enzyme intermediate [7] being formed during the catalytic cycle.

More information about this protein can be found at Protein of the Month: ATP Synthases [8].

Structural linksHelp
Database linksHelp
Enzyme: EC:3.6.3
Blocks: IPB000695

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000695 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A7L9Z8 Calcium-transporting ATPase type 2C member 2

O14983 Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

P05030 Plasma membrane ATPase 1

P19456 ATPase 2, plasma membrane-type

Q2QMX9 Calcium-transporting ATPase 1, plasma membrane-type

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code

PublicationsHelp
1. Cross RL, Muller V.
The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.
FEBS Lett. 576 1-4 2004 [PubMed: 15473999]
http://dx.doi.org/10.1016/j.febslet.2004.08.065
2. Rappas M, Niwa H, Zhang X.
Mechanisms of ATPases--a multi-disciplinary approach.
Curr. Protein Pept. Sci. 5 89-105 2004 [PubMed: 15078220]
http://dx.doi.org/10.2174/1389203043486874
3. Axelsen KB, Palmgren MG.
Evolution of substrate specificities in the P-type ATPase superfamily.
J. Mol. Evol. 46 84-101 1998 [PubMed: 9419228]
http://dx.doi.org/10.1007/PL00006286
4. Ewing NN, Wimmers LE, Meyer DJ, Chetelat RT, Bennett AB.
Molecular Cloning of Tomato Plasma Membrane H-ATPase.
Plant Physiol. 94 1874-1881 1990 [PubMed: 16667929]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=16667929&action=stream&blobtype=pdf
5. Harper JF, Manney L, DeWitt ND, Yoo MH, Sussman MR.
The Arabidopsis thaliana plasma membrane H(+)-ATPase multigene family. Genomic sequence and expression of a third isoform.
J. Biol. Chem. 265 13601-8 1990 [PubMed: 2143186]
http://intl.jbc.org/cgi/reprint/265/23/13601.pdf
6. Fagan MJ, Saier MH Jr.
P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees.
J. Mol. Evol. 38 57-99 1994 [PubMed: 8151716]
http://dx.doi.org/10.1007/BF00175496
7. Addison R.
Primary structure of the Neurospora plasma membrane H+-ATPase deduced from the gene sequence. Homology to Na+/K+-, Ca2+-, and K+-ATPase.
J. Biol. Chem. 261 14896-901 1986 [PubMed: 2876992]
http://intl.jbc.org/cgi/reprint/261/32/14896.pdf
8. McDowall J.
Protein of the Month - ATP Synthases.
2005

Additional ReadingHelp
Toyoshima C, Norimatsu Y, Iwasawa S, Tsuda T, Ogawa H.
How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 19831-6 [PubMed: 18077416]
http://dx.doi.org/10.1073/pnas.0709978104
Takahashi M, Kondou Y, Toyoshima C.
Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 5800-5 [PubMed: 17389383]
http://dx.doi.org/10.1073/pnas.0700979104
Jensen AM, Sorensen TL, Olesen C, Moller JV, Nissen P.
Modulatory and catalytic modes of ATP binding by the calcium pump.
EMBO J. 25 2006 2305-14 [PubMed: 16710301]
http://dx.doi.org/10.1038/sj.emboj.7601135
Sohoel H, Jensen AM, Moller JV, Nissen P, Denmeade SR, Isaacs JT, Olsen CE, Christensen SB.
Natural products as starting materials for development of second-generation SERCA inhibitors targeted towards prostate cancer cells.
Bioorg. Med. Chem. 14 2006 2810-5 [PubMed: 16412648]
http://dx.doi.org/10.1016/j.bmc.2005.12.001
Olesen C, Picard M, Winther AM, Gyrup C, Morth JP, Oxvig C, Moller JV, Nissen P.
The structural basis of calcium transport by the calcium pump.
Nature 450 2007 1036-42 [PubMed: 18075584]
http://dx.doi.org/10.1038/nature06418
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InterPro 23.1