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Links from Protein

Items: 10

1.

C-terminal domain of V and A type ATP synthase

Date:
2024-08-14
Family Accession:
NF047300.1
Method:
HMM
2.

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
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.

F0F1 ATP synthase subunit beta

F0F1 ATP synthase subunit beta is part of the catalytic core of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane and is found in bacterial, mitochondrial, and chloroplast membranes

Date:
2017-05-15
Family Accession:
11496593
Method:
Sparcle
9.

alternate F1F0 ATPase, F1 subunit beta

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 model represents the F1 beta subunit of this apparent second ATP synthase.

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)
Molecular Function:
proton-transporting ATP synthase activity, rotational mechanism (GO:0046933)
Molecular Function:
proton-transporting ATPase activity, rotational mechanism (GO:0046961)
Date:
2024-05-30
Family Accession:
TIGR03305.1
Method:
HMM
10.

F0F1 ATP synthase subunit beta

The F0F1 ATP synthase can produce ATP in the presence of a proton gradient across the membrane. Members of this family are the beta subunit of the F1 sector. The 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. Catalytic sites belong primarily to the beta-subunit.

Gene:
atpD
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:
TIGR01039.1
Method:
HMM
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