Q9C5A9 · ATPBO_ARATH
- ProteinATP synthase subunit beta-3, mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids559 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Catalytic activity
- ATP + 4 H+(in) + H2O = ADP + 5 H+(out) + phosphate
CHEBI:30616 + 4 H+ (in)CHEBI:15378+ CHEBI:15377 = CHEBI:456216 + 5 H+ (out)CHEBI:15378+ CHEBI:43474
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial proton-transporting ATP synthase complex | |
Cellular Component | mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) | |
Cellular Component | mitochondrion | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | copper ion binding | |
Molecular Function | proton-transporting ATP synthase activity, rotational mechanism | |
Molecular Function | proton-transporting ATPase activity, rotational mechanism |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP synthase subunit beta-3, mitochondrial
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9C5A9
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Peripheral membrane protein.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-54 | Mitochondrion | ||||
Sequence: MASRRILSSLLRSSSSRSTSKSSLIGSRNPRLLSPGPAHGAAPCGTLLGRVAEY | ||||||
Chain | PRO_0000045429 | 55-559 | ATP synthase subunit beta-3, mitochondrial | |||
Sequence: STSSPANSAAPSSAPAKDEGKKTYDYGGKGAIGRVCQVIGAIVDVRFEDQEGLPPIMTSLEVQDHPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKIAKESAA | ||||||
Modified residue | 62 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-29 | Polar residues | ||||
Sequence: MASRRILSSLLRSSSSRSTSKSSLIGSRN | ||||||
Region | 1-39 | Disordered | ||||
Sequence: MASRRILSSLLRSSSSRSTSKSSLIGSRNPRLLSPGPAH |
Sequence similarities
Belongs to the ATPase alpha/beta chains family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length559
- Mass (Da)59,859
- Last updated2001-06-01 v1
- ChecksumC14FD77E40F2EF37
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-29 | Polar residues | ||||
Sequence: MASRRILSSLLRSSSSRSTSKSSLIGSRN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL590346 EMBL· GenBank· DDBJ | CAC35873.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED91337.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117922 EMBL· GenBank· DDBJ | BAC42560.1 EMBL· GenBank· DDBJ | mRNA | ||
BT005920 EMBL· GenBank· DDBJ | AAO64855.1 EMBL· GenBank· DDBJ | mRNA |