Reviewed, UniProtKB/Swiss-Prot P00829 (ATPB_BOVIN)

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)

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 (F(1)F(O) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Catalytic activity	ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
Subunit structure	F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP catabolic process Inferred from mutant phenotype. Source: UniProtKB ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: InterPro mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW 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 hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro hydrogen ion transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 48

48

Mitochondrion

Chain

49 – 528

480

ATP synthase subunit beta, mitochondrial

PRO_0000002442

Regions

Nucleotide binding

206 – 213

8

ATP By similarity

Amino acid modifications

Modified residue

259

1

N6-acetyllysine By similarity

Modified residue

522

1

N6-acetyllysine By similarity

Natural variations

Natural variant

49 – 50

2

Missing in some mature chains.

Experimental info

Sequence conflict

182

1

I → L Ref.3 Ref.4

Sequence conflict

187

1

I → D Ref.3 Ref.4

Sequence conflict

196

1

Y → I in CAA29094. Ref.5

Sequence conflict

215

1

L → F Ref.3 Ref.4

Sequence conflict

274

1

E → Q Ref.3 Ref.4

Sequence conflict

338

1

D → N Ref.3 Ref.4

Sequence conflict

374

1

T → V Ref.3 Ref.4

Sequence conflict

409

1

D → N Ref.3 Ref.4

Secondary structure

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528

Helix Strand Turn

Details...

Beta strand

60 – 67

8

Beta strand

70 – 77

8

Beta strand

85 – 90

6

Beta strand

96 – 104

9

Beta strand

107 – 114

8

Beta strand

124 – 127

4

Beta strand

129 – 131

3

Beta strand

133 – 137

5

Helix

138 – 140

3

Beta strand

153 – 155

3

Beta strand

161 – 166

6

Helix

173 – 175

3

Helix

188 – 193

6

Beta strand

201 – 207

7

Helix

212 – 223

12

Turn

224 – 226

3

Beta strand

228 – 238

11

Helix

240 – 252

13

Beta strand

258 – 261

4

Beta strand

265 – 270

6

Helix

276 – 297

22

Beta strand

301 – 306

6

Helix

309 – 318

10

Turn

319 – 323

5

Helix

328 – 330

3

Helix

335 – 343

9

Beta strand

354 – 361

8

Helix

363 – 365

3

Helix

370 – 375

6

Helix

376 – 378

3

Beta strand

380 – 385

6

Helix

387 – 390

4

Turn

391 – 393

3

Helix

410 – 413

4

Helix

415 – 441

27

Helix

450 – 463

14

Helix

469 – 471

3

Helix

472 – 475

4

Helix

484 – 496

13

Turn

497 – 501

5

Helix

504 – 507

4

Helix

513 – 524

12

Sequences

	Sequence		Length	Mass (Da)
	P00829-1 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: 32218D14A5497F18	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

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: 2458129] [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: 6298222] [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: 2864455] [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: 2896550] [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: 1827992] [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: 1833193] [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: 6223927] [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: 2898218] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
[10]	"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: 8065448] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 48-528.
[11]	"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: 8790345] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 48-528.
[12]	"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: 9687365] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 48-528.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M20929 mRNA. Translation: AAA30395.1.
BC116099 mRNA. Translation: AAI16100.1.
X05605 mRNA. Translation: CAA29094.1.

PIR

PWBOB. A28717.

RefSeq

NP_786990.1.

UniGene

Bt.4431

3D structure databases

PDBMSD

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	47-528	[»]
1E1R	X-ray	2.50	D/E/F	47-528	[»]
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