Protein Domain : IPR008250

Type:  Domain Name:  P-type ATPase, A domain
Description:  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 [, ]. The different types include:F-ATPases (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 eukaryotic and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane []. They are also found in bacteria [].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 [, ].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) () are found in bacteria and in a number of eukaryotic plasma membranes and organelles []. 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 actuator (A) domain, and some transmembrane helices found in P-type ATPases []. It contains the TGES-loop which is essential for the metal ion binding which results in tight association between the A and P (phosphorylation) domains []. It does not contain the phosphorylation site. It is thought that the large movement of the actuator domain, which is transmitted to the transmembrane helices, is essential to the long distance coupling between formation/decomposition of the acyl phosphate in the cytoplasmic P-domainand the changes in the ion-binding sites buried deep in the membranous region []. This domain has a modulatory effect on the phosphoenzyme processing steps through its nucleotide binding [],[]. Short Name:  ATPase_P-typ_transduc_dom_A
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0 Child Features

0 Contains

2 Cross Referencess

Identifier
PF00122
G3DSA:2.70.150.10

10 Found Ins

DB identifier Type Name
IPR005782 Family P-type ATPase, subfamily IIA, SERCA-type
IPR001757 Family P-type ATPase
IPR006408 Family P-type ATPase, subfamily IIB
IPR006534 Family P-type ATPase, subfamily IIIA
IPR006544 Family P-type ATPase, subfamily V
IPR006415 Family P-type ATPase, subfamily IIIB
IPR006414 Family P-type ATPase, subfamily IID
IPR006391 Family P-type ATPase, B chain, subfamily IA
IPR006413 Family P-type ATPase, subfamily IIA, PMR1-type
IPR000579 Family Cation-transporting P-type ATPase A/B

2 GO Annotations

GO Term Gene Name
GO:0000166 IPR008250
GO:0046872 IPR008250

2 Ontology Annotations

GO Term Gene Name
GO:0000166 IPR008250
GO:0046872 IPR008250

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
231359 D8REZ4 PAC:15416074 Selaginella moellendorffii 924  
410847 D8RG22 PAC:15408698 Selaginella moellendorffii 1109  
92276 D8RFP0 PAC:15416970 Selaginella moellendorffii 953  
431418 D8TCK0 PAC:15422829 Selaginella moellendorffii 684  
78287 D8QUQ3 PAC:15420126 Selaginella moellendorffii 1062  
78895 D8QVR0 PAC:15402353 Selaginella moellendorffii 1041  
173214 PAC:15413263 Selaginella moellendorffii 1045  
149298 D8RRX0 PAC:15409342 Selaginella moellendorffii 781  
150274 D8RVE0 PAC:15412537 Selaginella moellendorffii 1095  
166180 D8QWP4 PAC:15414249 Selaginella moellendorffii 1039  
60775 D8QYH6 PAC:15415709 Selaginella moellendorffii 790  
417746 D8S3H3 PAC:15406071 Selaginella moellendorffii 322  
417745 D8S3H2 PAC:15406070 Selaginella moellendorffii 544  
233397 D8S8J9 PAC:15421876 Selaginella moellendorffii 817  
419690 D8S9Q9 PAC:15411356 Selaginella moellendorffii 1144  
113662 D8SCM4 PAC:15417813 Selaginella moellendorffii 1152  
167322 D8R2L0 PAC:15418477 Selaginella moellendorffii 817  
445084 D8SFF7 PAC:15416569 Selaginella moellendorffii 847  
445079 D8SFE9 PAC:15416537 Selaginella moellendorffii 1290  
118425 D8SJM4 PAC:15408435 Selaginella moellendorffii 831  
118764 D8SJW7 PAC:15410957 Selaginella moellendorffii 958  
84115 D8R2W8 PAC:15414789 Selaginella moellendorffii 960  
122320 D8SPX5 PAC:15419732 Selaginella moellendorffii 1018  
122175 D8SPR5 PAC:15418318 Selaginella moellendorffii 1011  
439526 D8R5P0 PAC:15402413 Selaginella moellendorffii 1246  
164122 D8QMQ3 PAC:15408058 Selaginella moellendorffii 1207  
129166 D8T0I2 PAC:15416398 Selaginella moellendorffii 904  
134300 D8T896 PAC:15410444 Selaginella moellendorffii 1101  
89397 D8RBL1 PAC:15408658 Selaginella moellendorffii 819  
76771 D8QT85 PAC:15418060 Selaginella moellendorffii 952  

12 Publications

First Author Title Year Journal Volume Pages PubMed ID
            15473999
            15078220
            9741106
            20450191
            18937357
            1385979
            9419228
            8226755
            15448704
            16710301
            18075584
            18930923