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GO:0016469
Overview
| Field | Value |
|---|---|
| Namespace | Cellular component |
| Short description | Proton-transporting two-sector ATPase complex |
| Full defintion | A large protein complex that catalyzes the synthesis or hydrolysis of ATP by a rotational mechanism, coupled to the transport of protons across a membrane. The complex comprises a membrane sector (F0, V0, or A0) that carries out proton transport and a cytoplasmic compartment sector (F1, V1, or A1) that catalyzes ATP synthesis or hydrolysis. Two major types have been characterized: V-type ATPases couple ATP hydrolysis to the transport of protons across a concentration gradient, whereas F-type ATPases, also known as ATP synthases, normally run in the reverse direction to utilize energy from a proton concentration or electrochemical gradient to synthesize ATP. A third type, A-type ATPases have been found in archaea, and are closely related to eukaryotic V-type ATPases but are reversible. |
| Subterm of |
Relationships
The relationship of GO:0016469 with other GO terms.
| Relationship type | GO terms |
|---|---|
| Is a | |
| Regulates | n.a. |
| Part of | n.a. |
| Positively regulates | n.a. |
| Negatively regulates | n.a. |
Ancestor tree
A force layout showing the ancestor tree for GO:0016469, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
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Additional data
This table contains additional metadata associated with the GO entry's definition field.
| Field | Value |
|---|---|
| GOC | mah |
| ISBN | Molecular Cell Biology Macmillan, 2004 · 1096 pages The fifth edition provides an authoritative and comprehensive vision of molecular biology today. It presents developments in cell birth, lineage and death, expanded coverage of signaling systems and of metabolism and movement of lipids. |
| PMID | ATP synthases with novel rotor subunits: new insights into structure, function and evolution of ATPases. J Bioenerg Biomembr. 2005 Dec; 37 (6): 455–60.PMID: 16691483 ATPases with unusual membrane-embedded rotor subunits were found in both F(1)F(0) and A(1)A(0) ATP synthases. The rotor subunit c of A(1)A(0) ATPases is, in most cases, similar to subunit c from F(0). Surprisingly, multiplied c subunits with four, six, or even 26 transmembrane spans have been found in some archaea and these multiplication events were sometimes accompanied by loss of the ion-translocating group. Nevertheless, these enzymes are still active as ATP synthases. A duplicated c subunit with only one ion-translocating group was found along with "normal" F(0) c subunits in the Na(+) F(1)F(0) ATP synthase of the bacterium Acetobacterium woodii. These extraordinary features and exceptional structural and functional variability in the rotor of ATP synthases may have arisen as an adaptation to different cellular needs and the extreme physicochemical conditions in the early history of life. |
Associated Lotus transcripts
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .