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P00829 (ATPB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit beta, mitochondrial

EC=3.6.3.14
Gene names
Name:ATP5B
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. HAMAP-Rule MF_01347

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_01347

Subunit structure

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 ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. Interacts with PPIF. 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 efficency. Ref.10 Ref.11

Subcellular location

Mitochondrion. Mitochondrion inner membrane. Note: Peripheral membrane protein. HAMAP-Rule MF_01347

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
   Biological processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCF(1)
Membrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB

ATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

ATP synthesis coupled proton transport

Inferred from electronic annotation. Source: InterPro

angiogenesis

Inferred from electronic annotation. Source: Ensembl

lipid metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell adhesion involved in substrate-bound cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of intracellular pH

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrial proton-transporting ATP synthase complex

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

proton-transporting ATP synthase complex, catalytic core F(1)

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 7397110. Source: UniProtKB

proton-transporting ATP synthase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Mitochondrion Ref.4 Ref.9
Chain49 – 528480ATP synthase subunit beta, mitochondrial HAMAP-Rule MF_01347
PRO_0000002442

Regions

Nucleotide binding206 – 2138ATP By similarity

Amino acid modifications

Modified residue1241N6-acetyllysine; alternate By similarity
Modified residue1241N6-succinyllysine; alternate By similarity
Modified residue1611N6-acetyllysine; alternate By similarity
Modified residue1611N6-succinyllysine; alternate By similarity
Modified residue1981N6-acetyllysine By similarity
Modified residue2591N6-acetyllysine; alternate By similarity
Modified residue2591N6-succinyllysine; alternate By similarity
Modified residue2641N6-acetyllysine; alternate By similarity
Modified residue2641N6-succinyllysine; alternate By similarity
Modified residue4261N6-acetyllysine By similarity
Modified residue4801N6-acetyllysine By similarity
Modified residue4851N6-acetyllysine By similarity
Modified residue5221N6-acetyllysine; alternate By similarity
Modified residue5221N6-succinyllysine; alternate By similarity

Natural variations

Natural variant49 – 502Missing in some mature chains.

Experimental info

Sequence conflict1821I → L AA sequence Ref.3
Sequence conflict1821I → L AA sequence Ref.4
Sequence conflict1871I → D AA sequence Ref.3
Sequence conflict1871I → D AA sequence Ref.4
Sequence conflict1961Y → I in CAA29094. Ref.5
Sequence conflict2151L → F AA sequence Ref.3
Sequence conflict2151L → F AA sequence Ref.4
Sequence conflict2741E → Q AA sequence Ref.3
Sequence conflict2741E → Q AA sequence Ref.4
Sequence conflict3381D → N AA sequence Ref.3
Sequence conflict3381D → N AA sequence Ref.4
Sequence conflict3741T → V AA sequence Ref.3
Sequence conflict3741T → V AA sequence Ref.4
Sequence conflict4091D → N AA sequence Ref.3
Sequence conflict4091D → N AA sequence Ref.4

Secondary structure

............................................................................................... 528
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00829 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 32218D14A5497F18

FASTA52856,284
        10         20         30         40         50         60 
MLGLVGRVVA ASASGALRGL SPSAPLPQAQ LLLRAAPAAL QPARDYAAQA SPSPKAGATT 

        70         80         90        100        110        120 
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV 

       130        140        150        160        170        180 
RGQKVLDSGA PIRIPVGPET LGRIMNVIGE PIDERGPIKT KQFAAIHAEA PEFVEMSVEQ 

       190        200        210        220        230        240 
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT 

       250        260        270        280        290        300 
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 

       310        320        330        340        350        360 
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI 

       370        380        390        400        410        420 
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV 

       430        440        450        460        470        480 
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHLGK 

       490        500        510        520 
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a complementary DNA for the nuclear-coded precursor of the beta-subunit of bovine mitochondrial F1-ATPase."
Breen G.A.M., Holmans P.L., Garnett K.E.
Biochemistry 27:3955-3961(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Ascending colon.
[3]"The amino acid sequence of the beta-subunit of ATP synthase from bovine heart mitochondria."
Runswick M.J., Walker J.E.
J. Biol. Chem. 258:3081-3089(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-528.
[4]"Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria."
Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.
J. Mol. Biol. 184:677-701(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 49-528.
[5]"Sequence analysis of cDNAs for the human and bovine ATP synthase beta subunit: mitochondrial DNA genes sustain seventeen times more mutations."
Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A., Greenberg B.D.
Curr. Genet. 12:81-90(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-528.
Tissue: Heart.
[6]"Identification of the subunits of F1F0-ATPase from bovine heart mitochondria."
Walker J.E., Lutter R., Dupuis A., Runswick M.J.
Biochemistry 30:5369-5378(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 47-55.
Tissue: Heart.
[7]"When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites."
Milgrom Y.M.
Eur. J. Biochem. 200:789-795(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 388-422.
Tissue: Heart.
[8]"The sites of labeling of the beta-subunit of bovine mitochondrial F1-ATPase with 8-azido-ATP."
Hollemans M., Runswick M.J., Fearnley I.M., Walker J.E.
J. Biol. Chem. 258:9307-9313(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: ATP-BINDING SITE.
[9]"Structural elucidation of N-terminal post-translational modifications by mass spectrometry: application to chicken enolase and the alpha- and beta-subunits of bovine mitochondrial F1-ATPase."
Gibson B.W., Daley D.J., Williams D.H.
Anal. Biochem. 169:217-226(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
[10]"Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
[11]"Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex."
Giorgio V., Bisetto E., Soriano M.E., Dabbeni-Sala F., Basso E., Petronilli V., Forte M.A., Bernardi P., Lippe G.
J. Biol. Chem. 284:33982-33988(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPIF.
[12]"Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria."
Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.
Nature 370:621-628(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 48-528.
[13]"The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin."
Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G., Walker J.E.
Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 48-528.
[14]"Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism."
Orriss G.L., Leslie A.G., Braig K., Walker J.E.
Structure 6:831-837(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 48-528.
[15]"The structure of bovine F1-ATPase in complex with its regulatory protein IF1."
Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.
Nat. Struct. Biol. 10:744-750(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATPIF1; ATP5A1 AND ATP5C1.
[16]"How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria."
Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.
Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5C1; ATP5D AND ATP5E.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20929 mRNA. Translation: AAA30395.1.
BC116099 mRNA. Translation: AAI16100.1.
X05605 mRNA. Translation: CAA29094.1.
PIRPWBOB. A28717.
RefSeqNP_786990.1. NM_175796.3.
UniGeneBt.4431.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMFX-ray2.85D/E/F47-528[»]
1COWX-ray3.10D/E/F47-528[»]
1E1QX-ray2.61D/E/F47-528[»]
1E1RX-ray2.50D/E/F47-528[»]
1E79X-ray2.40D/E/F47-528[»]
1EFRX-ray3.10D/E/F47-528[»]
1H8EX-ray2.00D/E/F47-528[»]
1H8HX-ray2.90D/E/F47-528[»]
1NBMX-ray3.00D/E/F47-526[»]
1OHHX-ray2.80D/E/F47-528[»]
1QO1X-ray3.90D/E/F47-525[»]
1W0JX-ray2.20D/E/F47-528[»]
1W0KX-ray2.85D/E/F47-528[»]
2CK3X-ray1.90D/E/F47-528[»]
2JDIX-ray1.90D/E/F47-528[»]
2JIZX-ray2.30D/E/F/K/L/M47-528[»]
2JJ1X-ray2.70D/E/F/K/L/M47-528[»]
2JJ2X-ray2.40D/E/F/K/L/M47-528[»]
2V7QX-ray2.10D/E/F47-528[»]
2W6EX-ray6.50D/E/F1-528[»]
2W6FX-ray6.00D/E/F1-528[»]
2W6GX-ray6.00D/E/F1-528[»]
2W6HX-ray5.00D/E/F1-528[»]
2W6IX-ray4.00D/E/F1-528[»]
2W6JX-ray3.84D/E/F1-528[»]
2WSSX-ray3.20D/E/F/M/N/O47-528[»]
2XNDX-ray3.50D/E/F59-525[»]
4ASUX-ray2.60D/E/F49-528[»]
ProteinModelPortalP00829.
SMRP00829. Positions 59-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35476N.
IntActP00829. 5 interactions.
MINTMINT-5006882.

Chemistry

ChEMBLCHEMBL612444.

Proteomic databases

PaxDbP00829.
PRIDEP00829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017710; ENSBTAP00000017710; ENSBTAG00000013315.
GeneID327675.
KEGGbta:327675.

Organism-specific databases

CTD506.

Phylogenomic databases

eggNOGCOG0055.
GeneTreeENSGT00550000074800.
HOGENOMHOG000009605.
HOVERGENHBG004307.
InParanoidP00829.
KOK02133.
OMANPAGQDV.
OrthoDBEOG73V6K6.
TreeFamTF105640.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01347. ATP_synth_beta_bact.
InterProIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01039. atpD. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00829.
NextBio20810140.

Entry information

Entry nameATPB_BOVIN
AccessionPrimary (citable) accession number: P00829
Secondary accession number(s): Q1JQA9, Q9T2U4, Q9T2U5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references