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Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5F1B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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.2 Publications

Catalytic activityi

ATP + H2O + 4 H+(Side 1) = ADP + phosphate + 4 H+(Side 2).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei239ATPCombined sources4 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi207 – 214ATPCombined sources4 Publications8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTranslocase
Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-1268020 Mitochondrial protein import
R-BTA-163210 Formation of ATP by chemiosmotic coupling
R-BTA-8949613 Cristae formation

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrialCurated (EC:7.1.2.2)
Alternative name(s):
ATP synthase F1 subunit betaBy similarity
Gene namesi
Name:ATP5F1BBy similarity
Synonyms:ATP5B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Organism-specific databases

VGNCiVGNC:26300 ATP5F1B

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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) serineBy 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 Expressed in 10 organ(s), highest expression level in heart

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 ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD 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 similarity8 Publications

GO - Molecular functioni

Protein-protein interaction databases

CORUMiP00829
DIPiDIP-35476N
IntActiP00829, 11 interactors
MINTiP00829
STRINGi9913.ENSBTAP00000017710

Chemistry databases

BindingDBiP00829

Structurei

Secondary structure

1528
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiFNMIMDG
OrthoDBiEOG091G0KVV
TreeFamiTF105640

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
HAMAPiMF_01347 ATP_synth_beta_bact, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01039 atpD, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit

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

Similar proteinsi

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

CORUMiP00829
DIPiDIP-35476N
IntActiP00829, 11 interactors
MINTiP00829
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
VGNCiVGNC:26300 ATP5F1B

Phylogenomic databases

eggNOGiKOG1350 Eukaryota
COG0055 LUCA
GeneTreeiENSGT00550000074800
HOGENOMiHOG000009605
HOVERGENiHBG004307
InParanoidiP00829
KOiK02133
OMAiFNMIMDG
OrthoDBiEOG091G0KVV
TreeFamiTF105640

Enzyme and pathway databases

ReactomeiR-BTA-1268020 Mitochondrial protein import
R-BTA-163210 Formation of ATP by chemiosmotic coupling
R-BTA-8949613 Cristae formation

Miscellaneous databases

EvolutionaryTraceiP00829
PROiPR:P00829

Gene expression databases

BgeeiENSBTAG00000013315 Expressed in 10 organ(s), highest expression level in heart

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
HAMAPiMF_01347 ATP_synth_beta_bact, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01039 atpD, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiATPB_BOVIN
AccessioniPrimary (citable) accession number: P00829
Secondary accession number(s): Q1JQA9, Q9T2U4, Q9T2U5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: November 7, 2018
This is version 187 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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