Protein Domain : IPR000793

Type:  Domain Name:  ATPase, F1/V1/A1 complex, alpha/beta subunit, C-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.The F-ATPases (or F1F0-ATPases), V-ATPases (or V1V0-ATPases) and A-ATPases (or A1A0-ATPases) are composed of two linked complexes: the F1, V1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0, V0 or A0 complex that forms the membrane-spanning pore. The F-, V- and A-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [, ].In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex, while the remaining F1 subunits (gamma, delta, epsilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits, those on the beta subunits being catalytic, while those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP, which are induced by the rotation of the gamma subunit, itself driven by the movement of protons through the F0 complex C subunit [].In V- and A-ATPases, the alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases, except that the alpha subunit is catalytic and the beta subunit is regulatory.The structure of the alpha and beta subunits is almost identical. Each subunit consists of a N-terminal beta-barrel, a central domain containing the nucleotide-binding site and a C-terminal alpha bundle domain []. This entry represents the C-terminal domain, which forms a left-handed superhelix composed of 4-5 individual helices. The C-terminal domain can vary between the alpha and beta subunits, and between different ATPases []. Short Name:  ATPase_F1/V1/A1-cplx_a/bsu_C
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1 Child Features

DB identifier Type Name
IPR024034 Domain ATPase, F1 complex beta subunit/V1 complex, C-terminal

0 Contains

2 Cross Referencess

Identifier
PF00306
SSF47917

7 Found Ins

DB identifier Type Name
IPR005725 Family ATPase, V1 complex, subunit A
IPR005722 Family ATPase, F1 complex, beta subunit
IPR005294 Family ATPase, F1 complex, alpha subunit
IPR005724 Family ATPase, A1 complex, beta subunit
IPR005726 Family ATP synthase alpha chain, archaea
IPR017691 Family ATP synthase subunit beta, bacterial and archaeal
IPR017710 Family Alternate F1F0 ATPase, F1 subunit alpha

3 GO Annotations

GO Term Gene Name
GO:0016820 IPR000793
GO:0015991 IPR000793
GO:0033178 IPR000793

3 Ontology Annotations

GO Term Gene Name
GO:0016820 IPR000793
GO:0015991 IPR000793
GO:0033178 IPR000793

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
236855 D8TE87 PAC:15412156 Selaginella moellendorffii 451  
137834 C7B2E9 PAC:15422935 Selaginella moellendorffii 506  
167777 D8R3X7 PAC:15421544 Selaginella moellendorffii 591  
269014 D8SQC5 PAC:15414084 Selaginella moellendorffii 480  
139657 D8QQX5 PAC:15405011 Selaginella moellendorffii 427  
1752 PAC:15409376 Selaginella moellendorffii 488  
evm.TU.contig_30366.2 PAC:16429811 Carica papaya 83  
evm.model.supercontig_155.13 PAC:16409732 Carica papaya 623  
evm.model.supercontig_20.109 PAC:16412903 Carica papaya 488  
evm.model.supercontig_20.110 PAC:16412905 Carica papaya 431  
evm.model.supercontig_65.97 PAC:16424511 Carica papaya 560  
29852.m001987 B9RL04 PAC:16811549 Ricinus communis 111  
29869.m001165 B9S5J4 PAC:16811889 Ricinus communis 406  
29923.m000788 B9SD14 PAC:16813644 Ricinus communis 207  
29923.m000792 B9SD18 PAC:16813648 Ricinus communis 265  
30063.m001448 B9S087 PAC:16816405 Ricinus communis 424  
30169.m006261 B9RHV0 PAC:16821064 Ricinus communis 573  
30170.m014284 B9R8F3 PAC:16822117 Ricinus communis 488  
50378.m000013 B9TBB1 PAC:16828261 Ricinus communis 487  
52479.m000014 B9TBD5 PAC:16828527 Ricinus communis 362  
28565.m000334 B9T1V8 PAC:16801112 Ricinus communis 561  
Cucsa.368130.1 PAC:16981659 Cucumis sativus 306  
Cucsa.358070.1 PAC:16980452 Cucumis sativus 222  
Cucsa.280580.1 A0A0A0KPJ2 PAC:16974233 Cucumis sativus 560  
Cucsa.283140.1 A0A0A0KTA5 PAC:16974492 Cucumis sativus 558  
Cucsa.359540.2 PAC:16980587 Cucumis sativus 547  
Cucsa.359540.1 A0A0A0K6R4 PAC:16980586 Cucumis sativus 623  
Cucsa.370360.1 PAC:16981754 Cucumis sativus 488  
orange1.1g011348m A0A067FXK2 PAC:18099441 Citrus sinensis 488  
orange1.1g011350m A0A067FXK2 PAC:18099439 Citrus sinensis 488  

10 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11309608
            15473999
            15078220
            9741106
            20450191
            18937357
            1385979
            8065448
            15629643
            12745923