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Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5B

Organism
Bos taurus (Bovine)
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 bindingi206 – 213ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.
R-BTA-2151201. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:ATP5B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL612444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 48Mitochondrion2 PublicationsAdd BLAST48
ChainiPRO_000000244249 – 528ATP synthase subunit beta, mitochondrialAdd BLAST480

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi106O-linked (GlcNAc)By similarity1
Modified residuei124N6-acetyllysine; alternateBy similarity1
Modified residuei124N6-succinyllysine; alternateBy similarity1
Modified residuei161N6-acetyllysine; alternateBy similarity1
Modified residuei161N6-succinyllysine; alternateBy similarity1
Modified residuei198N6-acetyllysineBy similarity1
Modified residuei259N6-acetyllysine; alternateBy similarity1
Modified residuei259N6-succinyllysine; alternateBy similarity1
Modified residuei264N6-acetyllysine; alternateBy similarity1
Modified residuei264N6-succinyllysine; alternateBy similarity1
Modified residuei312PhosphothreonineBy similarity1
Modified residuei415PhosphoserineBy similarity1
Modified residuei426N6-acetyllysineBy similarity1
Modified residuei433PhosphoserineBy similarity1
Modified residuei480N6-acetyllysineBy similarity1
Modified residuei485N6-acetyllysineBy similarity1
Modified residuei522N6-acetyllysine; alternateBy similarity1
Modified residuei522N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP00829.
PeptideAtlasiP00829.
PRIDEiP00829.

Expressioni

Gene expression databases

BgeeiENSBTAG00000013315.

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. 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 (PubMed:17570365, PubMed:12923572, PubMed:17895376). Interacts with PPIF (PubMed:19801635). 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. Interacts with CLN5 and PPT1 (By similarity).By similarity4 Publications

Protein-protein interaction databases

DIPiDIP-35476N.
IntActiP00829. 5 interactors.
MINTiMINT-5006882.
STRINGi9913.ENSBTAP00000017710.

Chemistry databases

BindingDBiP00829.

Structurei

Secondary structure

1528
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 67Combined sources8
Beta strandi70 – 77Combined sources8
Beta strandi85 – 90Combined sources6
Beta strandi96 – 104Combined sources9
Beta strandi107 – 114Combined sources8
Beta strandi124 – 127Combined sources4
Beta strandi129 – 131Combined sources3
Beta strandi133 – 135Combined sources3
Helixi138 – 140Combined sources3
Beta strandi147 – 149Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi163 – 166Combined sources4
Helixi173 – 175Combined sources3
Helixi188 – 193Combined sources6
Beta strandi201 – 206Combined sources6
Beta strandi208 – 211Combined sources4
Helixi212 – 223Combined sources12
Turni224 – 226Combined sources3
Beta strandi228 – 237Combined sources10
Helixi240 – 252Combined sources13
Beta strandi254 – 256Combined sources3
Beta strandi258 – 261Combined sources4
Beta strandi265 – 270Combined sources6
Helixi276 – 295Combined sources20
Beta strandi297 – 299Combined sources3
Beta strandi301 – 306Combined sources6
Helixi309 – 319Combined sources11
Helixi320 – 322Combined sources3
Helixi328 – 330Combined sources3
Helixi335 – 343Combined sources9
Beta strandi346 – 348Combined sources3
Beta strandi349 – 351Combined sources3
Beta strandi354 – 361Combined sources8
Helixi363 – 365Combined sources3
Helixi370 – 375Combined sources6
Helixi376 – 378Combined sources3
Beta strandi380 – 385Combined sources6
Helixi387 – 390Combined sources4
Turni391 – 393Combined sources3
Turni400 – 402Combined sources3
Beta strandi404 – 407Combined sources4
Helixi410 – 413Combined sources4
Helixi415 – 441Combined sources27
Helixi443 – 445Combined sources3
Helixi448 – 464Combined sources17
Helixi469 – 471Combined sources3
Helixi472 – 475Combined sources4
Helixi484 – 495Combined sources12
Turni496 – 501Combined sources6
Helixi504 – 507Combined sources4
Helixi513 – 524Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4TSFX-ray3.20D/E/F49-528[»]
4TT3X-ray3.21D/E/F49-528[»]
4YXWX-ray3.10D/E/F47-528[»]
4Z1MX-ray3.30D/E/F47-528[»]
5ARAelectron microscopy6.70D/E/F47-528[»]
5AREelectron microscopy7.40D/E/F47-528[»]
5ARHelectron microscopy7.20D/E/F47-528[»]
5ARIelectron microscopy7.40D/E/F47-528[»]
5FIJelectron microscopy7.40D/E/F47-528[»]
5FIKelectron microscopy6.40D/E/F47-528[»]
5FILelectron microscopy7.10D/E/F47-528[»]
ProteinModelPortaliP00829.
SMRiP00829.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00829.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
GeneTreeiENSGT00550000074800.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP00829.
KOiK02133.
OMAiAEFGIYP.
OrthoDBiEOG091G0KVV.
TreeFamiTF105640.

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.

P00829-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGLVGRVVA ASASGALRGL SPSAPLPQAQ LLLRAAPAAL QPARDYAAQA
60 70 80 90 100
SPSPKAGATT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA
110 120 130 140 150
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIRIPVGPET LGRIMNVIGE
160 170 180 190 200
PIDERGPIKT KQFAAIHAEA PEFVEMSVEQ EILVTGIKVV DLLAPYAKGG
210 220 230 240 250
KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM
260 270 280 290 300
IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
310 320 330 340 350
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK
360 370 380 390 400
KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP
410 420 430 440 450
LDSTSRIMDP NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED
460 470 480 490 500
KLTVSRARKI QRFLSQPFQV AEVFTGHLGK LVPLKETIKG FQQILAGEYD
510 520
HLPEQAFYMV GPIEEAVAKA DKLAEEHS
Length:528
Mass (Da):56,284
Last modified:January 1, 1990 - v2
Checksum:i32218D14A5497F18
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti182I → L AA sequence (PubMed:6298222).Curated1
Sequence conflicti182I → L AA sequence (PubMed:2864455).Curated1
Sequence conflicti187I → D AA sequence (PubMed:6298222).Curated1
Sequence conflicti187I → D AA sequence (PubMed:2864455).Curated1
Sequence conflicti196Y → I in CAA29094 (PubMed:2896550).Curated1
Sequence conflicti215L → F AA sequence (PubMed:6298222).Curated1
Sequence conflicti215L → F AA sequence (PubMed:2864455).Curated1
Sequence conflicti274E → Q AA sequence (PubMed:6298222).Curated1
Sequence conflicti274E → Q AA sequence (PubMed:2864455).Curated1
Sequence conflicti338D → N AA sequence (PubMed:6298222).Curated1
Sequence conflicti338D → N AA sequence (PubMed:2864455).Curated1
Sequence conflicti374T → V AA sequence (PubMed:6298222).Curated1
Sequence conflicti374T → V AA sequence (PubMed:2864455).Curated1
Sequence conflicti409D → N AA sequence (PubMed:6298222).Curated1
Sequence conflicti409D → N AA sequence (PubMed:2864455).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti49 – 50Missing in some mature chains. 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20929 mRNA. Translation: AAA30395.1.
BC116099 mRNA. Translation: AAI16100.1.
X05605 mRNA. Translation: CAA29094.1.
PIRiA28717. PWBOB.
RefSeqiNP_786990.1. NM_175796.3.
UniGeneiBt.4431.

Genome annotation databases

EnsembliENSBTAT00000017710; ENSBTAP00000017710; ENSBTAG00000013315.
GeneIDi327675.
KEGGibta:327675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20929 mRNA. Translation: AAA30395.1.
BC116099 mRNA. Translation: AAI16100.1.
X05605 mRNA. Translation: CAA29094.1.
PIRiA28717. PWBOB.
RefSeqiNP_786990.1. NM_175796.3.
UniGeneiBt.4431.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4TSFX-ray3.20D/E/F49-528[»]
4TT3X-ray3.21D/E/F49-528[»]
4YXWX-ray3.10D/E/F47-528[»]
4Z1MX-ray3.30D/E/F47-528[»]
5ARAelectron microscopy6.70D/E/F47-528[»]
5AREelectron microscopy7.40D/E/F47-528[»]
5ARHelectron microscopy7.20D/E/F47-528[»]
5ARIelectron microscopy7.40D/E/F47-528[»]
5FIJelectron microscopy7.40D/E/F47-528[»]
5FIKelectron microscopy6.40D/E/F47-528[»]
5FILelectron microscopy7.10D/E/F47-528[»]
ProteinModelPortaliP00829.
SMRiP00829.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35476N.
IntActiP00829. 5 interactors.
MINTiMINT-5006882.
STRINGi9913.ENSBTAP00000017710.

Chemistry databases

BindingDBiP00829.
ChEMBLiCHEMBL612444.

Proteomic databases

PaxDbiP00829.
PeptideAtlasiP00829.
PRIDEiP00829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017710; ENSBTAP00000017710; ENSBTAG00000013315.
GeneIDi327675.
KEGGibta:327675.

Organism-specific databases

CTDi506.

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
GeneTreeiENSGT00550000074800.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP00829.
KOiK02133.
OMAiAEFGIYP.
OrthoDBiEOG091G0KVV.
TreeFamiTF105640.

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.
R-BTA-2151201. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

EvolutionaryTraceiP00829.
PROiP00829.

Gene expression databases

BgeeiENSBTAG00000013315.

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_BOVIN
AccessioniPrimary (citable) accession number: P00829
Secondary accession number(s): Q1JQA9, Q9T2U4, Q9T2U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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.