The domain within your query sequence starts at position 2 and ends at position 42; the E-value for the H-K_ATPase_N domain shown below is 4.9e-28.

GKAENYELYSVELGSGPGGDMTAKMSKKKAGGGGGKKKEKL

H-K_ATPase_N

H-K_ATPase_N
PFAM accession number:PF09040
Interpro abstract (IPR015127):

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing 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.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [(PUBMED:15473999), (PUBMED:15078220)]. The different types include:

  • F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [(PUBMED:20450191)]. They are also found in bacteria [(PUBMED:9741106)].
  • A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [(PUBMED:18937357), (PUBMED:1385979)].
  • P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

P-ATPases (also known as E1-E2 ATPases) (EC 3.6.3.-) are found in bacteria and in a number of eukaryotic plasma membranes and organelles [(PUBMED:9419228)]. 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, which transport specific types 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.

This entry represents the N-terminal domain found in gastric H+/K+-transporter ATPases. This domain adopts an alpha-helical conformation under hydrophobic conditions. The domain contains tyrosine residues, phosphorylation of which regulates the function of the ATPase. Additionally, the domain also interacts with various structural proteins, including the spectrin-binding domain of ankyrin III [(PUBMED:12480547)].

GO process:ATP hydrolysis coupled proton transport (GO:0015991)
GO component:membrane (GO:0016020)
GO function:magnesium ion binding (GO:0000287), ATP binding (GO:0005524), potassium:proton exchanging ATPase activity (GO:0008900)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry H-K_ATPase_N