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Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi190 – 197ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled proton transport Source: SGD
  • protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31742-MONOMER.
BRENDAi3.6.3.14. 984.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:ATP2
Ordered Locus Names:YJR121W
ORF Names:J2041
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR121W.
SGDiS000003882. ATP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 33MitochondrionAdd BLAST33
ChainiPRO_000000245434 – 511ATP synthase subunit beta, mitochondrialAdd BLAST478

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112PhosphothreonineCombined sources1
Modified residuei237PhosphothreonineCombined sources1
Modified residuei373PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00830.
PRIDEiP00830.

2D gel databases

SWISS-2DPAGEP00830.

PTM databases

iPTMnetiP00830.

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

WithEntry#Exp.IntActNotes
INA17Q028882EBI-3242,EBI-7668387

Protein-protein interaction databases

BioGridi33877. 76 interactors.
DIPiDIP-3028N.
IntActiP00830. 71 interactors.
MINTiMINT-534087.

Chemistry databases

BindingDBiP00830.

Structurei

Secondary structure

1511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 50Combined sources8
Beta strandi53 – 58Combined sources6
Beta strandi59 – 61Combined sources3
Beta strandi69 – 72Combined sources4
Beta strandi75 – 77Combined sources3
Beta strandi79 – 88Combined sources10
Beta strandi91 – 98Combined sources8
Beta strandi108 – 111Combined sources4
Beta strandi113 – 115Combined sources3
Beta strandi117 – 119Combined sources3
Helixi122 – 124Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi131 – 133Combined sources3
Beta strandi137 – 139Combined sources3
Beta strandi147 – 150Combined sources4
Helixi157 – 159Combined sources3
Helixi172 – 177Combined sources6
Beta strandi180 – 183Combined sources4
Beta strandi184 – 190Combined sources7
Beta strandi192 – 195Combined sources4
Helixi196 – 207Combined sources12
Turni208 – 210Combined sources3
Beta strandi211 – 213Combined sources3
Beta strandi215 – 222Combined sources8
Helixi224 – 235Combined sources12
Turni236 – 238Combined sources3
Beta strandi242 – 244Combined sources3
Beta strandi247 – 253Combined sources7
Helixi259 – 278Combined sources20
Beta strandi283 – 289Combined sources7
Helixi292 – 302Combined sources11
Helixi303 – 305Combined sources3
Helixi311 – 313Combined sources3
Helixi318 – 326Combined sources9
Beta strandi332 – 334Combined sources3
Beta strandi335 – 344Combined sources10
Helixi346 – 348Combined sources3
Helixi353 – 358Combined sources6
Helixi359 – 361Combined sources3
Beta strandi363 – 368Combined sources6
Helixi370 – 374Combined sources5
Turni383 – 385Combined sources3
Helixi393 – 396Combined sources4
Helixi398 – 423Combined sources26
Helixi426 – 428Combined sources3
Helixi431 – 446Combined sources16
Helixi455 – 458Combined sources4
Helixi467 – 479Combined sources13
Turni480 – 484Combined sources5
Helixi487 – 489Combined sources3
Turni490 – 492Combined sources3
Helixi496 – 507Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.80D/E/F/M/N/O/V/W/X34-511[»]
2WPDX-ray3.43D/E/F34-511[»]
2XOKX-ray3.01D/E/F1-507[»]
3FKSX-ray3.59D/E/F/M/N/O/V/W/X36-511[»]
3OE7X-ray3.19D/E/F/M/N/O/V/W/X36-511[»]
3OEEX-ray2.74D/E/F/M/N/O/V/W/X36-511[»]
3OEHX-ray3.00D/E/F/M/N/O/V/W/X36-511[»]
3OFNX-ray3.20D/E/F/M/N/O/V/W/X36-511[»]
3ZIAX-ray2.50D/E/F/N/O/P34-511[»]
3ZRYX-ray6.50D/E/F34-511[»]
4B2Qelectron microscopy37.00D/d39-508[»]
E/F/e/f39-511[»]
ProteinModelPortaliP00830.
SMRiP00830.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00830.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000074800.
HOGENOMiHOG000009605.
InParanoidiP00830.
KOiK02133.
OMAiHDHISEN.
OrthoDBiEOG092C1U90.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00830-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:511
Mass (Da):54,794
Last modified:December 20, 2005 - v2
Checksum:iEDFF256826F68F0C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti201Q → M in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti218T → A in AAA34444 (PubMed:2866186).Curated1
Sequence conflicti218T → A in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti232 – 237REMKET → HEMEDS in AAA34443 (PubMed:6225776).Curated6
Sequence conflicti260G → E in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti287 – 288FI → Y in AAA34443 (PubMed:6225776).Curated2
Sequence conflicti354 – 358APATT → SPSTS in AAA34444 (PubMed:2866186).Curated5
Sequence conflicti365 – 366TT → SS in AAA34444 (PubMed:2866186).Curated2
Sequence conflicti365 – 366TT → SS in AAA34443 (PubMed:6225776).Curated2
Sequence conflicti469 – 473DTVAS → RTRCL in AAA34443 (PubMed:6225776).Curated5
Sequence conflicti489A → R in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti501A → R in AAA34444 (PubMed:2866186).Curated1
Sequence conflicti508A → R in AAA34444 (PubMed:2866186).Curated1

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.
PIRiS57144. PWBYB.
RefSeqiNP_012655.3. NM_001181779.3.

Genome annotation databases

EnsemblFungiiYJR121W; YJR121W; YJR121W.
GeneIDi853585.
KEGGisce:YJR121W.

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.
PIRiS57144. PWBYB.
RefSeqiNP_012655.3. NM_001181779.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.80D/E/F/M/N/O/V/W/X34-511[»]
2WPDX-ray3.43D/E/F34-511[»]
2XOKX-ray3.01D/E/F1-507[»]
3FKSX-ray3.59D/E/F/M/N/O/V/W/X36-511[»]
3OE7X-ray3.19D/E/F/M/N/O/V/W/X36-511[»]
3OEEX-ray2.74D/E/F/M/N/O/V/W/X36-511[»]
3OEHX-ray3.00D/E/F/M/N/O/V/W/X36-511[»]
3OFNX-ray3.20D/E/F/M/N/O/V/W/X36-511[»]
3ZIAX-ray2.50D/E/F/N/O/P34-511[»]
3ZRYX-ray6.50D/E/F34-511[»]
4B2Qelectron microscopy37.00D/d39-508[»]
E/F/e/f39-511[»]
ProteinModelPortaliP00830.
SMRiP00830.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33877. 76 interactors.
DIPiDIP-3028N.
IntActiP00830. 71 interactors.
MINTiMINT-534087.

Chemistry databases

BindingDBiP00830.
ChEMBLiCHEMBL1075103.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

iPTMnetiP00830.

2D gel databases

SWISS-2DPAGEP00830.

Proteomic databases

MaxQBiP00830.
PRIDEiP00830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR121W; YJR121W; YJR121W.
GeneIDi853585.
KEGGisce:YJR121W.

Organism-specific databases

EuPathDBiFungiDB:YJR121W.
SGDiS000003882. ATP2.

Phylogenomic databases

GeneTreeiENSGT00550000074800.
HOGENOMiHOG000009605.
InParanoidiP00830.
KOiK02133.
OMAiHDHISEN.
OrthoDBiEOG092C1U90.

Enzyme and pathway databases

BioCyciYEAST:G3O-31742-MONOMER.
BRENDAi3.6.3.14. 984.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiP00830.
PROiP00830.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATPB_YEAST
AccessioniPrimary (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: November 30, 2016
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 164000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.