Protein Domain : IPR020546

Type:  Domain Name:  ATPase, F1 complex, delta/epsilon subunit, N-terminal
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.F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) () are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis []. These ATPases can also work in reverse in bacteria, hydrolysing ATP to create a proton gradient.This family represents subunits called delta (in mitochondrial ATPase) or epsilon (in bacteria or chloroplast ATPase). The interaction site of subunit C of the F0 complex with the delta or epsilon subunit of the F1 complex may be important for connecting the rotor of F1 (gamma subunit) to the rotor of F0 (C subunit) []. In bacterial species, the delta subunit is the equivalent of the Oligomycin sensitive subunit (OSCP, ) in metazoans. The C-terminal domain of the epsilon subunit appears to act as an inhibitor of ATPase activity []. Short Name:  ATPase_F1-cplx_dsu/esu_N

0 Child Features

0 Contains

4 Cross Referencess

Identifier
PF02823
PD000944
G3DSA:2.60.15.10
SSF51344

1 Found In

DB identifier Type Name
IPR001469 Family ATPase, F1 complex, delta/epsilon subunit

4 GO Annotations

GO Term Gene Name
GO:0046933 IPR020546
GO:0046961 IPR020546
GO:0015986 IPR020546
GO:0045261 IPR020546

4 Ontology Annotations

GO Term Gene Name
GO:0046933 IPR020546
GO:0046961 IPR020546
GO:0015986 IPR020546
GO:0045261 IPR020546

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
137774 C7B2G0 PAC:15422281 Selaginella moellendorffii 143  
184168 D8R026 PAC:15422630 Selaginella moellendorffii 215  
evm.model.supercontig_106.98 PAC:16405268 Carica papaya 204  
30174.m008837 B9RD81 PAC:16822482 Ricinus communis 161  
29628.m000785 B9SS29 PAC:16803928 Ricinus communis 204  
Cucsa.256900.1 A0A0A0L7T8 PAC:16972622 Cucumis sativus 200  
orange1.1g029006m A0A067ECC5 PAC:18123523 Citrus sinensis 200  
orange1.1g041201m A0A067HC41 PAC:18137594 Citrus sinensis 94  
AT5G47030.1 Q96252 PAC:19667926 Arabidopsis thaliana 203  
ATCG00470.1 P09468 PAC:19637994 Arabidopsis thaliana 132  
Thhalv10011087m V4L6H9 PAC:20206830 Eutrema salsugineum 531  
Thhalv10001028m V4KPL8 PAC:20202640 Eutrema salsugineum 203  
Ciclev10022328m V4TNV1 PAC:20809046 Citrus clementina 200  
Ciclev10026896m V4SVL3 PAC:20800900 Citrus clementina 70  
Lus10001082 PAC:23148929 Linum usitatissimum 206  
Lus10040130 PAC:23173895 Linum usitatissimum 206  
Lus10011038 PAC:23148691 Linum usitatissimum 1091  
Potri.009G029700.1 A0A2K1Z1W9 PAC:26988028 Populus trichocarpa 76  
Potri.003G086100.1 A9PD87 PAC:26999999 Populus trichocarpa 207  
Potri.007G021100.1 A0A2K1ZMZ8 PAC:27014763 Populus trichocarpa 71  
Potri.007G054600.1 A0A2K1ZPS1 PAC:27015003 Populus trichocarpa 70  
Potri.014G053000.1 B9MV35 PAC:27034177 Populus trichocarpa 198  
Gorai.001G177300.1 A0A0D2Q0B1 PAC:26822093 Gossypium raimondii 202  
Gorai.003G067400.1 A0A0D2NXB5 PAC:26800105 Gossypium raimondii 92  
Gorai.004G068100.1 A0A0D2MUM7 PAC:26774337 Gossypium raimondii 200  
Gorai.004G068100.2 A0A0D2MUM7 PAC:26774338 Gossypium raimondii 200  
Gorai.004G167800.1 A0A0D2S113 PAC:26772258 Gossypium raimondii 201  
Gorai.008G191800.1 A0A0D2T323 PAC:26812623 Gossypium raimondii 68  
Gorai.008G229700.2 A0A0D2Q040 PAC:26817310 Gossypium raimondii 201  
Gorai.008G229700.1 A0A0D2RKP0 PAC:26817309 Gossypium raimondii 202  

9 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11309608
            15473999
            15078220
            9741106
            20450191
            18937357
            1385979
            12887009
            16707672