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Links from Protein

Items: 12

1.

ATP synthase alpha/beta family, beta-barrel domain

This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella. [1]. 8065448. Structure at 2.8 A resolution of F1-ATPase from bovine heart. mitochondria.. Abrahams JP, Leslie AG, Lutter R, Walker JE;. Nature 1994;370:621-628.. [2]. 9261073. The crystal structure of the nucleotide-free alpha 3 beta 3. subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a. symmetric trimer.. Shirakihara Y, Leslie AG, Abrahams JP, Walker JE, Ueda T,. Sekimoto Y, Kambara M, Saika K, Kagawa Y, Yoshida M;. Structure 1997;5:825-836. (from Pfam)

GO Terms:
Biological Process:
ATP metabolic process (GO:0046034)
Biological Process:
proton transmembrane transport (GO:1902600)
Date:
2024-08-14
Family Accession:
NF014873.5
Method:
HMM
2.

ATP synthase alpha/beta chain, C terminal domain

GO Terms:
Biological Process:
proton motive force-driven ATP synthesis (GO:0015986)
Date:
2024-08-14
Family Accession:
NF012527.5
Method:
HMM
3.

ATP synthase alpha/beta family, nucleotide-binding domain

This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho. [1]. 8065448. Structure at 2.8 A resolution of F1-ATPase from bovine heart. mitochondria.. Abrahams JP, Leslie AG, Lutter R, Walker JE;. Nature 1994;370:621-628.. [2]. 9261073. The crystal structure of the nucleotide-free alpha 3 beta 3. subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a. symmetric trimer.. Shirakihara Y, Leslie AG, Abrahams JP, Walker JE, Ueda T,. Sekimoto Y, Kambara M, Saika K, Kagawa Y, Yoshida M;. Structure 1997;5:825-836. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Date:
2024-08-14
Family Accession:
NF012236.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
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9.
new record, indexing in progress
Family Accession:
10.

F0F1 ATP synthase subunit alpha

Produces ATP from ADP in the presence of a proton gradient across the membrane; the alpha chain is a catalytic subunit

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
proton motive force-driven ATP synthesis (GO:0015986)
Cellular Component:
proton-transporting ATP synthase complex, catalytic core F(1) (GO:0045261)
Molecular Function:
proton-transporting ATP synthase activity, rotational mechanism (GO:0046933)
Date:
2022-02-18
Family Accession:
NF009884.0
Method:
HMM
11.

F0F1 ATP synthase subunit alpha

F0F1 ATP synthase subunit alpha is part of the catalytic core of the F-ATPase that uses a proton gradient to drive ATP synthesis; it hydrolyzes ATP to build the proton gradient and is found in bacterial, mitochondrial, and chloroplast membranes

Date:
2023-03-13
Family Accession:
11483744
Method:
Sparcle
12.

F0F1 ATP synthase subunit alpha

The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit.

Gene:
atpA
GO Terms:
Biological Process:
proton motive force-driven ATP synthesis (GO:0015986)
Cellular Component:
proton-transporting ATP synthase complex, catalytic core F(1) (GO:0045261)
Cellular Component:
plasma membrane proton-transporting ATP synthase complex, catalytic core F(1) (GO:0045262)
Molecular Function:
proton-transporting ATP synthase activity, rotational mechanism (GO:0046933)
Date:
2024-06-27
Family Accession:
TIGR00962.1
Method:
HMM
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