UniProtKB - P00830 (ATPB_YEAST)
ATP synthase subunit beta, mitochondrial
ATP2
Functioni
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.
Miscellaneous
Catalytic activityi
- EC:7.1.2.2
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 190 – 197 | ATPBy similarity | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- proton-transporting ATPase activity, rotational mechanism Source: SGD
- proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB-EC
GO - Biological processi
- ATP synthesis coupled proton transport Source: SGD
- mitochondrial ATP synthesis coupled proton transport Source: GO_Central
Keywordsi
Molecular function | Translocase |
Biological process | ATP synthesis, Hydrogen ion transport, Ion transport, Transport |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 7.1.2.2, 984 |
Reactomei | R-SCE-163210, Formation of ATP by chemiosmotic coupling R-SCE-8949613, Cristae formation |
Protein family/group databases
TCDBi | 3.A.2.1.3, the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ATP2 Ordered Locus Names:YJR121W ORF Names:J2041 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000003882, ATP2 |
VEuPathDBi | FungiDB:YJR121W |
Subcellular locationi
Mitochondrion
Note: Peripheral membrane protein.
Cytosol
- cytosol Source: Reactome
Mitochondrion
- mitochondrial inner membrane Source: ComplexPortal
- mitochondrial intermembrane space Source: Reactome
- mitochondrial proton-transporting ATP synthase complex Source: GO_Central
- mitochondrial proton-transporting ATP synthase, catalytic core Source: SGD
- mitochondrion Source: SGD
Other locations
Keywords - Cellular componenti
CF(1), Membrane, Mitochondrion, Mitochondrion inner membranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 33 | MitochondrionAdd BLAST | 33 | |
ChainiPRO_0000002454 | 34 – 511 | ATP synthase subunit beta, mitochondrialAdd BLAST | 478 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 112 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 237 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 373 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | P00830 |
PaxDbi | P00830 |
PRIDEi | P00830 |
2D gel databases
SWISS-2DPAGEi | P00830 |
PTM databases
iPTMneti | P00830 |
Interactioni
Subunit structurei
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.
Binary interactionsi
P00830
With | #Exp. | IntAct |
---|---|---|
INA17 [Q02888] | 2 | EBI-3242,EBI-7668387 |
Protein-protein interaction databases
BioGRIDi | 33877, 232 interactors |
ComplexPortali | CPX-3281, Mitochondrial proton-transporting ATP synthase complex |
DIPi | DIP-3028N |
IntActi | P00830, 177 interactors |
MINTi | P00830 |
STRINGi | 4932.YJR121W |
Chemistry databases
BindingDBi | P00830 |
Miscellaneous databases
RNActi | P00830, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P00830 |
SMRi | P00830 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P00830 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG1350, Eukaryota |
GeneTreei | ENSGT00550000074800 |
HOGENOMi | CLU_022398_0_2_1 |
InParanoidi | P00830 |
OMAi | GFNMIMD |
Family and domain databases
Gene3Di | 1.10.1140.10, 1 hit 3.40.50.300, 1 hit |
HAMAPi | MF_01347, ATP_synth_beta_bact, 1 hit |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR005722, ATP_synth_F1_bsu IPR020003, ATPase_a/bsu_AS IPR004100, ATPase_F1/V1/A1_a/bsu_N IPR036121, ATPase_F1/V1/A1_a/bsu_N_sf IPR000194, ATPase_F1/V1/A1_a/bsu_nucl-bd IPR024034, ATPase_F1/V1_b/a_C IPR027417, P-loop_NTPase |
Pfami | View protein in Pfam PF00006, ATP-synt_ab, 1 hit PF02874, ATP-synt_ab_N, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF50615, SSF50615, 1 hit SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR01039, atpD, 1 hit |
PROSITEi | View protein in PROSITE PS00152, ATPASE_ALPHA_BETA, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MVLPRLYTAT SRAAFKAAKQ SAPLLSTSWK RCMASAAQST PITGKVTAVI
60 70 80 90 100
GAIVDVHFEQ SELPAILNAL EIKTPQGKLV LEVAQHLGEN TVRTIAMDGT
110 120 130 140 150
EGLVRGEKVL DTGGPISVPV GRETLGRIIN VIGEPIDERG PIKSKLRKPI
160 170 180 190 200
HADPPSFAEQ STSAEILETG IKVVDLLAPY ARGGKIGLFG GAGVGKTVFI
210 220 230 240 250
QELINNIAKA HGGFSVFTGV GERTREGNDL YREMKETGVI NLEGESKVAL
260 270 280 290 300
VFGQMNEPPG ARARVALTGL TIAEYFRDEE GQDVLLFIDN IFRFTQAGSE
310 320 330 340 350
VSALLGRIPS AVGYQPTLAT DMGLLQERIT TTKKGSVTSV QAVYVPADDL
360 370 380 390 400
TDPAPATTFA HLDATTVLSR GISELGIYPA VDPLDSKSRL LDAAVVGQEH
410 420 430 440 450
YDVASKVQET LQTYKSLQDI IAILGMDELS EQDKLTVERA RKIQRFLSQP
460 470 480 490 500
FAVAEVFTGI PGKLVRLKDT VASFKAVLEG KYDNIPEHAF YMVGGIEDVV
510
AKAEKLAAEA N
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 201 | Q → M in AAA34443 (PubMed:6225776).Curated | 1 | |
Sequence conflicti | 218 | T → A in AAA34444 (PubMed:2866186).Curated | 1 | |
Sequence conflicti | 218 | T → A in AAA34443 (PubMed:6225776).Curated | 1 | |
Sequence conflicti | 232 – 237 | REMKET → HEMEDS in AAA34443 (PubMed:6225776).Curated | 6 | |
Sequence conflicti | 260 | G → E in AAA34443 (PubMed:6225776).Curated | 1 | |
Sequence conflicti | 287 – 288 | FI → Y in AAA34443 (PubMed:6225776).Curated | 2 | |
Sequence conflicti | 354 – 358 | APATT → SPSTS in AAA34444 (PubMed:2866186).Curated | 5 | |
Sequence conflicti | 365 – 366 | TT → SS in AAA34444 (PubMed:2866186).Curated | 2 | |
Sequence conflicti | 365 – 366 | TT → SS in AAA34443 (PubMed:6225776).Curated | 2 | |
Sequence conflicti | 469 – 473 | DTVAS → RTRCL in AAA34443 (PubMed:6225776).Curated | 5 | |
Sequence conflicti | 489 | A → R in AAA34443 (PubMed:6225776).Curated | 1 | |
Sequence conflicti | 501 | A → R in AAA34444 (PubMed:2866186).Curated | 1 | |
Sequence conflicti | 508 | A → R in AAA34444 (PubMed:2866186).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M12082 Genomic DNA Translation: AAA34444.1 U46215 Genomic DNA Translation: AAC49475.1 Z49621 Genomic DNA Translation: CAA89652.1 X52004 Genomic DNA Translation: CAA36255.1 K00560 Genomic DNA Translation: AAA34443.1 BK006943 Genomic DNA Translation: DAA08906.1 |
PIRi | S57144, PWBYB |
RefSeqi | NP_012655.3, NM_001181779.3 |
Genome annotation databases
EnsemblFungii | YJR121W_mRNA; YJR121W; YJR121W |
GeneIDi | 853585 |
KEGGi | sce:YJR121W |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M12082 Genomic DNA Translation: AAA34444.1 U46215 Genomic DNA Translation: AAC49475.1 Z49621 Genomic DNA Translation: CAA89652.1 X52004 Genomic DNA Translation: CAA36255.1 K00560 Genomic DNA Translation: AAA34443.1 BK006943 Genomic DNA Translation: DAA08906.1 |
PIRi | S57144, PWBYB |
RefSeqi | NP_012655.3, NM_001181779.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2HLD | X-ray | 2.80 | D/E/F/M/N/O/V/W/X | 34-511 | [»] | |
2WPD | X-ray | 3.43 | D/E/F | 34-511 | [»] | |
2XOK | X-ray | 3.01 | D/E/F | 1-507 | [»] | |
3FKS | X-ray | 3.59 | D/E/F/M/N/O/V/W/X | 36-511 | [»] | |
3OE7 | X-ray | 3.19 | D/E/F/M/N/O/V/W/X | 36-511 | [»] | |
3OEE | X-ray | 2.74 | D/E/F/M/N/O/V/W/X | 36-511 | [»] | |
3OEH | X-ray | 3.00 | D/E/F/M/N/O/V/W/X | 36-511 | [»] | |
3OFN | X-ray | 3.20 | D/E/F/M/N/O/V/W/X | 36-511 | [»] | |
3ZIA | X-ray | 2.50 | D/E/F/N/O/P | 34-511 | [»] | |
3ZRY | X-ray | 6.50 | D/E/F | 34-511 | [»] | |
4B2Q | electron microscopy | 37.00 | D/d | 39-508 | [»] | |
E/F/e/f | 39-511 | [»] | ||||
6B8H | electron microscopy | 3.60 | D/E/F/Y/Z/c | 34-511 | [»] | |
6CP3 | electron microscopy | 3.80 | D/E/F | 34-511 | [»] | |
6CP6 | electron microscopy | 3.60 | D/E/F | 34-511 | [»] | |
AlphaFoldDBi | P00830 | |||||
SMRi | P00830 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 33877, 232 interactors |
ComplexPortali | CPX-3281, Mitochondrial proton-transporting ATP synthase complex |
DIPi | DIP-3028N |
IntActi | P00830, 177 interactors |
MINTi | P00830 |
STRINGi | 4932.YJR121W |
Chemistry databases
BindingDBi | P00830 |
ChEMBLi | CHEMBL1075103 |
Protein family/group databases
TCDBi | 3.A.2.1.3, the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily |
PTM databases
iPTMneti | P00830 |
2D gel databases
SWISS-2DPAGEi | P00830 |
Proteomic databases
MaxQBi | P00830 |
PaxDbi | P00830 |
PRIDEi | P00830 |
Genome annotation databases
EnsemblFungii | YJR121W_mRNA; YJR121W; YJR121W |
GeneIDi | 853585 |
KEGGi | sce:YJR121W |
Organism-specific databases
SGDi | S000003882, ATP2 |
VEuPathDBi | FungiDB:YJR121W |
Phylogenomic databases
eggNOGi | KOG1350, Eukaryota |
GeneTreei | ENSGT00550000074800 |
HOGENOMi | CLU_022398_0_2_1 |
InParanoidi | P00830 |
OMAi | GFNMIMD |
Enzyme and pathway databases
BRENDAi | 7.1.2.2, 984 |
Reactomei | R-SCE-163210, Formation of ATP by chemiosmotic coupling R-SCE-8949613, Cristae formation |
Miscellaneous databases
ChiTaRSi | ATP2, yeast |
EvolutionaryTracei | P00830 |
PROi | PR:P00830 |
RNActi | P00830, protein |
Family and domain databases
Gene3Di | 1.10.1140.10, 1 hit 3.40.50.300, 1 hit |
HAMAPi | MF_01347, ATP_synth_beta_bact, 1 hit |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR005722, ATP_synth_F1_bsu IPR020003, ATPase_a/bsu_AS IPR004100, ATPase_F1/V1/A1_a/bsu_N IPR036121, ATPase_F1/V1/A1_a/bsu_N_sf IPR000194, ATPase_F1/V1/A1_a/bsu_nucl-bd IPR024034, ATPase_F1/V1_b/a_C IPR027417, P-loop_NTPase |
Pfami | View protein in Pfam PF00006, ATP-synt_ab, 1 hit PF02874, ATP-synt_ab_N, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF50615, SSF50615, 1 hit SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR01039, atpD, 1 hit |
PROSITEi | View protein in PROSITE PS00152, ATPASE_ALPHA_BETA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ATPB_YEAST | |
Accessioni | P00830Primary (citable) accession number: P00830 Secondary accession number(s): D6VWU0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | December 20, 2005 | |
Last modified: | May 25, 2022 | |
This is version 223 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome X
Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families