Subsystem: V-Type ATP synthase

This subsystem's description is:

For more information, please check out the description and the additional notes tabs, below

Literature ReferencesV-Type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon. Yokoyama K The Journal of biological chemistry 2000 May 510788522
Rotation, structure, and classification of prokaryotic V-ATPase. Yokoyama K Journal of bioenergetics and biomembranes 2005 Dec16691473
The cellular biology of proton-motive force generation by V-ATPases. Nelson N The Journal of experimental biology 2000 Jan10600677
DiagramFunctional RolesSubsystem SpreadsheetAdditional Notes 

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Group Alias
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ABCDEFGIK*H
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Notes copied from V-Type_ATP_synthase_2:
Notes copied from V-Type_ATP_synthase:
Overview:

F-type H+-ATPase (FoF1) and vacuolar type H+-ATPase (VoV1) are two classes of a superfamily of H+-translocating ATPases FoF1 is responsible for ATP synthesis and is present in inner membranes of mitochondria, thylakoid membranes of chloroplasts, and plasma membranes of bacteria. VoV1 is present in the membranes of yeast vacuoles,clathrin-coated vesicles, chromaffine granules (8), lysosomes, and plant vacuoles in eukaryotic cells, and it pumps H+ into vesicles. Like FoF1, the VoV1 is composed of a water-soluble set of subunits (V1) and a membrane-integral set of subunits (Vo). The two major A and B subunits and other minor subunits comprise the V1 domain. The A and B subunits are homologous to the and subunits of FoF1. By analogy to F1, V1 has also been proposed to have a central shaft subunit that rotates in the A3B3 hexagon. However, an equivalent subunit with indisputable sequence homology to the F1 subunit has not been identified in VoV1. The hydrophobic Vo is thought to be composed of at least five different subunits. The 16-kDa proteolipid subunit containing four transmembrane domains is the major subunit of Vo. Unlike FoF1, V1 dissociates into individual subunits with concomitant loss of ATPase activity, and Vo does not show activity as a H+ channel by itself once V1 is detached from Vo.
Based on SDS-polyacrylamide gel electrophoresis (PAGE),1 the isolated T. thermophilus VoV1 has been thought to be composed of eight kinds of polypeptides with the following apparent molecular sizes: 100, 66, 56, 38, 30, 24, 13, and 12 kDa. Four of them, A (66 kDa), B (56 kDa), (30 kDa), and (12 kDa), are found in the purified V1, whereas the 100-, 38-, 24-, and 13-kDa polypeptides are thought to be Vo subunits.
J Biol Chem, Vol. 275, Issue 18, 13955-13961, May 5, 2000
V-Type H+-ATPase/Synthase from a Thermophilic Eubacterium, Thermus Thermophilus
SUBUNIT STRUCTURE AND OPERON*
Ken Yokoyama§, Shoji Ohkuma, Hideki Taguchi¶, Takuo Yasunaga, Takeyuki Wakabayashi, and Masasuke Yoshida (http://www.jbc.org/cgi/content/full/275/18/13955)

Variant codes:
1-complete set of subunits (G subunit)
2-complete set of subunits (H subunit)
3-complete set of subunits (archaean H subunit)
4-G/H/Ha-missing (??)

SubunitH-atoH gene
Archaean H-ntpF in Thermoplasma acidophilum