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Items: 9

1.

C-terminal domain of V and A type ATP synthase

This entry represents a small alpha helical domain found at the C-terminus of a variety of ATP synthases. Paper describing PDB structure 1fx0. [1]. 11032839. The structure of the chloroplast F1-ATPase at 3.2 A resolution. Groth G, Pohl E;. J Biol Chem. 2001;276:1345-1352. Paper describing PDB structure 1mab. [2]. 9736690. The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis. Bianchet MA, Hullihen J, Pedersen PL, Amzel LM;. Proc Natl Acad Sci U S A. 1998;95:11065-11070. Paper describing PDB structure 1nbm. [3]. 9687365. Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism. Orriss GL, Leslie AG, Braig K, Walker JE;. Structure. 1998;6:831-837. (from Pfam)

Date:
2024-10-16
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:
2024-10-16
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:
2024-10-16
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:
2024-07-16
Family Accession:
11414600
Method:
Sparcle
9.

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)
Molecular Function:
proton-transporting ATP synthase activity, rotational mechanism (GO:0046933)
Date:
2024-10-21
Family Accession:
TIGR01039.1
Method:
HMM
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