F
IPR024037

Alternate ATP synthase, F1 complex, subunit epsilon

InterPro entry
Short nameAlt_ATP_synth_F1_esu
Overlapping
homologous
superfamilies
 
family relationships

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.

A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This entry represents the F1 epsilon subunit of this apparent second ATP synthase
[1]
.

References

1.F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri. Sumi M, Yohda M, Koga Y, Yoshida M. Biochem. Biophys. Res. Commun. 241, 427-33, (1997). View articlePMID: 9425287

Further reading

2. Mechanisms of ATPases--a multi-disciplinary approach. Rappas M, Niwa H, Zhang X. Curr. Protein Pept. Sci. 5, 89-105, (2004). View articlePMID: 15078220

3. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. Cross RL, Muller V. FEBS Lett. 576, 1-4, (2004). View articlePMID: 15473999

4. F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. Schafer G, Meyering-Vos M. Biochim. Biophys. Acta 1101, 232-5, (1992). PMID: 1385979

5. Regulation and isoform function of the V-ATPases. Toei M, Saum R, Forgac M. Biochemistry 49, 4715-23, (2010). View articlePMID: 20450191

6. New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). Gruber G, Marshansky V. Bioessays 30, 1096-109, (2008). View articlePMID: 18937357

7. F-and V-ATPases in the genus Thermus and related species. Radax C, Sigurdsson O, Hreggvidsson GO, Aichinger N, Gruber C, Kristjansson JK, Stan-Lotter H. Syst. Appl. Microbiol. 21, 12-22, (1998). PMID: 9741106

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