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P-ATPase

1wpg opm.png
Calcium ATPase, E2-Pi state
Identifiers
Symbol E1-E2_ATPase
Pfam PF00122
InterPro IPR008250
PROSITE PDOC00139
SCOP 1su4
SUPERFAMILY 1su4
TCDB 3.A.3
OPM superfamily 22
OPM protein 3b9b
Cation transporting ATPase, C-terminus
PDB 1vfp EBI.jpg
crystal structure of the sr ca2+-atpase with bound amppcp
Identifiers
Symbol Cation_ATPase_C
Pfam PF00689
InterPro IPR006068
SCOP 1eul
SUPERFAMILY 1eul
TCDB 3.A.3
Cation transporter/ATPase, N-terminus
PDB 1mhs EBI.jpg
model of neurospora crassa proton atpase
Identifiers
Symbol Cation_ATPase_N
Pfam PF00690
InterPro IPR004014
SCOP 1eul
SUPERFAMILY 1eul
TCDB 3.A.3

The P-type ATPases, also known as E1-E2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. P-type ATPases fall under the P-type ATPase (P-ATPase) Superfamily (TC# 3.A.3) which, as of early 2016, includes 20 different protein families. P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation of a key conserved aspartate residue within the pump and their energy source, adenosine triphosphate (ATP). In addition, they all appear to interconvert between at least two different conformations, denoted by E1 and E2.

Most members of this transporter superfamily catalyze cation uptake and/or efflux, however one subfamily (TC# 3.A.3.8) is involved in flipping phospholipids to maintain the asymmetric nature of the biomembrane.

Prominent examples of P-type ATPases are the sodium-potassium pump (Na+/K+-ATPase), the plasma membrane proton pump (H+-ATPase), the proton-potassium pump (H+/K+-ATPase), and the calcium pump (Ca2+-ATPase).

The first P-type ATPase discovered was the Na+/K+-ATPase, which Nobel laureate Jens Christian Skou isolated in 1957. The Na+/K+-ATPase was only the first member of a large and still-growing protein family (see Swiss-Prot Prosite motif PS00154).


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