Protein Domain : IPR006415

Type:  Family Name:  P-type ATPase, subfamily IIIB
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 group describes the magnesium translocating P-type ATPase found in a limited number of bacterial species and best described in Salmonella typhimurium, which contains two isoforms []. These transporters are active in low external Mg2+ concentrations and pump the ion into the cytoplasm. The magnesium ATPases have been classified as type IIIB by a phylogenetic analysis []. Short Name:  P-type_ATPase_IIIB

0 Child Features

3 Contains

DB identifier Type Name
IPR008250 Domain P-type ATPase, A domain
IPR004014 Domain Cation-transporting P-type ATPase, N-terminal
IPR018303 PTM P-type ATPase, phosphorylation site

3 Cross Referencess

Identifier
PTHR24093:SF128
PR01836
TIGR01524

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0015444 IPR006415
GO:0015693 IPR006415
GO:0016021 IPR006415

3 Ontology Annotations

GO Term Gene Name
GO:0015444 IPR006415
GO:0015693 IPR006415
GO:0016021 IPR006415

0 Parent Features

245 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
evm.model.supercontig_55.62 PAC:16422630 Carica papaya 938  
29810.m000144 B9T5P6 PAC:16809368 Ricinus communis 863  
orange1.1g045750m A0A067FB16 PAC:18139389 Citrus sinensis 792  
Ciclev10027273m V4SG35 PAC:20799519 Citrus clementina 957  
Potri.005G147900.1 PAC:27030592 Populus trichocarpa 761  
Potri.007G010100.1 A0A2K1ZM76 PAC:27016973 Populus trichocarpa 107  
Gorai.007G235300.3 A0A0D2PE24 PAC:26783310 Gossypium raimondii 921  
Gorai.007G235300.1 A0A0D2SIR9 PAC:26783309 Gossypium raimondii 953  
Gorai.007G235300.4 A0A0D2SQA5 PAC:26783312 Gossypium raimondii 770  
Gorai.007G235300.2 A0A0D2TK73 PAC:26783311 Gossypium raimondii 865  
Thecc1EG001029t1 A0A061DIC0 PAC:27435537 Theobroma cacao 953  
Thecc1EG001029t2 A0A061DIC0 PAC:27435538 Theobroma cacao 953  
Glyma.05G175300.2.p A0A0R0JX21 PAC:30524107 Glycine max 948  
Glyma.05G175300.4.p K7KQV4 PAC:30524108 Glycine max 863  
Glyma.05G175300.1.p A0A0R0JX32 PAC:30524106 Glycine max 965  
Glyma.05G175300.3.p K7KQV4 PAC:30524109 Glycine max 863  
Glyma.08G132600.1.p K7L6G0 PAC:30537220 Glycine max 752  
Glyma.08G132600.2.p K7L6G0 PAC:30537219 Glycine max 752  
Medtr8g089870.1 A0A072TTD6 PAC:31071167 Medicago truncatula 873  
SapurV1A.0513s0030.2.p PAC:31429116 Salix purpurea 793  
SapurV1A.0513s0030.4.p PAC:31429118 Salix purpurea 710  
SapurV1A.0513s0030.1.p PAC:31429115 Salix purpurea 945  
SapurV1A.0513s0030.5.p PAC:31429119 Salix purpurea 664  
SapurV1A.0513s0030.3.p PAC:31429117 Salix purpurea 793  
Spipo15G0017800 PAC:31507180 Spirodela polyrhiza 782  
Spipo15G0017900 PAC:31507111 Spirodela polyrhiza 136  
evm_27.model.AmTr_v1.0_scaffold00008.112 W1NIM9 PAC:31569476 Amborella trichopoda 944  
Eucgr.H04736.1.p A0A059B8T1 PAC:32044607 Eucalyptus grandis 947  
Prupe.6G194600.3.p A0A251NVG9 PAC:32088774 Prunus persica 790  
Prupe.6G194600.2.p A0A251NVG9 PAC:32088773 Prunus persica 790  

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            15473999
            15078220
            9741106
            20450191
            18937357
            1385979
            9419228
            1328179