Protein Family Models

The HAS barrel is named after HerA-ATP Synthase. In ATP synthases, this domain is implicated in the assembly of the catalytic toroid and docking of accessory subunits, such as the subunit of the ATP synthase complex. Similar roles in docking of the functional partner, the NurA nuclease, and assembly of the HerA toroid complex appear likely for the HAS-barrel of the HerA family [1]. [1]. 15466593. Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Iyer LM, Makarova KS, Koonin EV, Aravind L;. Nucleic Acids Res. 2004;32:5260-5279. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

Date:

2024-08-14

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)

Date:

2024-10-16

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

Date:

2022-02-18

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:

2024-11-17

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

Date:

2024-10-21