P00829 · ATPB_BOVIN
- ProteinATP synthase subunit beta, mitochondrial
- GeneATP5F1B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids528 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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) + phosphateThis reaction proceeds in the backward direction.
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 | mitochondrion | |
Cellular Component | proton-transporting ATP synthase complex | |
Cellular Component | proton-transporting ATP synthase complex, catalytic core F(1) | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | proton-transporting ATP synthase activity, rotational mechanism | |
Molecular Function | proton-transporting ATPase activity, rotational mechanism | |
Biological Process | proton motive force-driven mitochondrial ATP synthesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP synthase subunit beta, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP00829
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 49-50 | in some mature chains | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-46 | Mitochondrion | ||||
Sequence: MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDY | ||||||
Chain | PRO_0000002442 | 47-528 | ATP synthase subunit beta, mitochondrial | |||
Sequence: AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS | ||||||
Glycosylation | 106 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 124 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 124 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 161 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 161 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 198 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 259 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 259 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 264 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 264 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 312 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 415 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 426 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 433 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 480 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 485 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 522 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 522 | N6-succinyllysine; alternate | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (PubMed:12923572, PubMed:17570365, PubMed:17895376, PubMed:25851905).
Interacts with PPIF (PubMed:19801635).
Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficiency. Interacts with CLN5 and PPT1 (By similarity).
Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity).
Interacts with MTLN (By similarity).
Interacts with TTC5/STRAP; the interaction results in decreased mitochondrial ATP production (By similarity).
Interacts with PPIF (PubMed:19801635).
Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficiency. Interacts with CLN5 and PPT1 (By similarity).
Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity).
Interacts with MTLN (By similarity).
Interacts with TTC5/STRAP; the interaction results in decreased mitochondrial ATP production (By similarity).
Protein-protein interaction databases
Chemistry
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length528
- Mass (Da)56,284
- Last updated1990-01-01 v2
- Checksum32218D14A5497F18
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 182 | in Ref. 3; AA sequence and 4; AA sequence | ||||
Sequence: I → L | ||||||
Sequence conflict | 187 | in Ref. 3; AA sequence and 4; AA sequence | ||||
Sequence: I → D | ||||||
Sequence conflict | 196 | in Ref. 5; CAA29094 | ||||
Sequence: Y → I | ||||||
Sequence conflict | 215 | in Ref. 3; AA sequence and 4; AA sequence | ||||
Sequence: L → F | ||||||
Sequence conflict | 274 | in Ref. 3; AA sequence and 4; AA sequence | ||||
Sequence: E → Q | ||||||
Sequence conflict | 338 | in Ref. 3; AA sequence and 4; AA sequence | ||||
Sequence: D → N | ||||||
Sequence conflict | 374 | in Ref. 3; AA sequence and 4; AA sequence | ||||
Sequence: T → V | ||||||
Sequence conflict | 409 | in Ref. 3; AA sequence and 4; AA sequence | ||||
Sequence: D → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M20929 EMBL· GenBank· DDBJ | AAA30395.1 EMBL· GenBank· DDBJ | mRNA | ||
BC116099 EMBL· GenBank· DDBJ | AAI16100.1 EMBL· GenBank· DDBJ | mRNA | ||
X05605 EMBL· GenBank· DDBJ | CAA29094.1 EMBL· GenBank· DDBJ | mRNA |