ATP synthase subunit beta, mitochondrial precursor

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P00829 (ATPB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 137. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP synthase subunit beta, mitochondrial
EC=3.6.3.14

Gene names

Name:

ATP5B

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Catalytic activity	ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out).
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. Ref.10 Ref.11
Subcellular location	Mitochondrion. Mitochondrion inner membrane. Note: Peripheral membrane protein.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP 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: Compara lipid metabolic process Inferred from electronic annotation. Source: Compara negative regulation of cell adhesion involved in substrate-bound cell migration Inferred from electronic annotation. Source: Compara regulation of intracellular pH Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara mitochondrial nucleoid Inferred from electronic annotation. Source: Compara mitochondrial proton-transporting ATP synthase complex Inferred from direct assay Ref.10. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW eukaryotic cell surface binding Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 48

Mitochondrion Ref.4 Ref.9

Chain

49 – 528

480

ATP synthase subunit beta, mitochondrial

PRO_0000002442

Regions

Nucleotide binding

206 – 213

ATP By similarity

Amino acid modifications

Modified residue

198

N6-acetyllysine By similarity

Modified residue

259

N6-acetyllysine By similarity

Modified residue

426

N6-acetyllysine By similarity

Modified residue

522

N6-acetyllysine By similarity

Natural variations

Natural variant

49 – 50

Missing in some mature chains.

Experimental info

Sequence conflict

182

I → L AA sequence Ref.3

Sequence conflict

182

I → L AA sequence Ref.4

Sequence conflict

187

I → D AA sequence Ref.3

Sequence conflict

187

I → D AA sequence Ref.4

Sequence conflict

196

Y → I in CAA29094. Ref.5

Sequence conflict

215

L → F AA sequence Ref.3

Sequence conflict

215

L → F AA sequence Ref.4

Sequence conflict

274

E → Q AA sequence Ref.3

Sequence conflict

274

E → Q AA sequence Ref.4

Sequence conflict

338

D → N AA sequence Ref.3

Sequence conflict

338

D → N AA sequence Ref.4

Sequence conflict

374

T → V AA sequence Ref.3

Sequence conflict

374

T → V AA sequence Ref.4

Sequence conflict

409

D → N AA sequence Ref.3

Sequence conflict

409

D → N AA sequence Ref.4

Secondary structure

528

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00829 [UniParc].

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

FASTA

528

56,284

        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' referencesShow '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.

IPI

IPI00717884.

PIR

PWBOB. A28717.

RefSeq

NP_786990.1. NM_175796.3.

UniGene

Bt.4431.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BMF	X-ray	2.85	D/E/F	47-528	[»]
1COW	X-ray	3.10	D/E/F	47-528	[»]
1E1Q	X-ray	2.61	D/E/F	47-525	[»]
1E1R	X-ray	2.50	D/E/F	47-525	[»]
1E79	X-ray	2.40	D/E/F	47-528	[»]
1EFR	X-ray	3.10	D/E/F	47-528	[»]
1H8E	X-ray	2.00	D/E/F	47-528	[»]
1H8H	X-ray	2.90	D/E/F	47-528	[»]
1NBM	X-ray	3.00	D/E/F	47-526	[»]
1OHH	X-ray	2.80	D/E/F	47-528	[»]
1QO1	X-ray	3.90	D/E/F	47-528	[»]
1W0J	X-ray	2.20	D/E/F	47-528	[»]
1W0K	X-ray	2.85	D/E/F	47-528	[»]
2CK3	X-ray	1.90	D/E/F	47-528	[»]
2JDI	X-ray	1.90	D/E/F	47-528	[»]
2JIZ	X-ray	2.30	D/E/F/K/L/M	47-528	[»]
2JJ1	X-ray	2.70	D/E/F/K/L/M	47-528	[»]
2JJ2	X-ray	2.40	D/E/F/K/L/M	47-528	[»]
2V7Q	X-ray	2.10	D/E/F	47-528	[»]
2W6E	X-ray	6.50	D/E/F	1-528	[»]
2W6F	X-ray	6.00	D/E/F	1-528	[»]
2W6G	X-ray	6.00	D/E/F	1-528	[»]
2W6H	X-ray	5.00	D/E/F	1-528	[»]
2W6I	X-ray	4.00	D/E/F	1-528	[»]
2W6J	X-ray	3.84	D/E/F	1-528	[»]
2WSS	X-ray	3.20	D/E/F/M/N/O	47-528	[»]
2XND	X-ray	3.50	D/E/F	59-525	[»]
4ASU	X-ray	2.60	D/E/F	49-528	[»]

ProteinModelPortal

P00829.

SMR

P00829. Positions 59-527.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35476N.

IntAct

P00829. 4 interactions.

MINT

MINT-5006882.

Proteomic databases

PaxDb

P00829.

PRIDE

P00829.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000017710; ENSBTAP00000017710; ENSBTAG00000013315.

GeneID

327675.

KEGG

bta:327675.

Organism-specific databases

CTD

506.

Phylogenomic databases

eggNOG

COG0055.

GeneTree

ENSGT00550000074800.

HOGENOM

HOG000009605.

HOVERGEN

HBG004307.

InParanoid

P00829.

K02133.

OMA

NNIAKGH.

OrthoDB

EOG4ZCT4C.

Family and domain databases

Gene3D

1.10.1140.10. 1 hit.

InterPro

IPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1_bsu/V1_C.
[Graphical view]

PANTHER

PTHR15184:SF8. PTHR15184:SF8. 1 hit.

Pfam

PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.

TIGRFAMs

TIGR01039. atpD. 1 hit.

PROSITE

PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00829.

NextBio

20810140.

Entry information

Entry name

ATPB_BOVIN

Accession

Primary (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:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents