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Protein

ATP synthase subunit beta, mitochondrial

Gene

Atp5b

Organism
Rattus norvegicus (Rat)
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

  • ATPase activity Source: RGD
  • ATP binding Source: RGD
  • calcium ion binding Source: RGD
  • lipoprotein particle receptor activity Source: RGD
  • proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  • ATP metabolic process Source: RGD
  • ATP synthesis coupled proton transport Source: InterPro
  • receptor-mediated endocytosis Source: RGD
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

BRENDAi3.6.3.14. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:Atp5b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621368. Atp5b.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: RGD
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
  • mitochondrion Source: RGD
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 46Mitochondrion1 PublicationAdd BLAST46
ChainiPRO_000000244547 – 529ATP synthase subunit beta, mitochondrialAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi106O-linked (GlcNAc)1 Publication1
Modified residuei124N6-acetyllysine; alternateBy similarity1
Modified residuei124N6-succinyllysine; alternateBy similarity1
Modified residuei133N6-acetyllysine; alternateBy similarity1
Modified residuei133N6-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 residuei433PhosphoserineCombined sources1
Modified residuei480N6-acetyllysineBy similarity1
Modified residuei485N6-acetyllysineBy similarity1
Modified residuei522N6-acetyllysine; alternateBy similarity1
Modified residuei522N6-succinyllysine; alternateBy similarity1
Modified residuei529PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP10719.
PRIDEiP10719.

2D gel databases

UCD-2DPAGEP10719.
World-2DPAGE0004:P10719.

PTM databases

iPTMnetiP10719.
PhosphoSitePlusiP10719.

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:17575325). Interacts with PPIF (By similarity). 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 (PubMed:21926988). Interacts with CLN5 and PPT1 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi251212. 4 interactors.
IntActiP10719. 7 interactors.
MINTiMINT-4587159.
STRINGi10116.ENSRNOP00000003965.

Structurei

Secondary structure

1529
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 62Combined sources3
Beta strandi65 – 67Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi75 – 77Combined sources3
Beta strandi85 – 90Combined sources6
Beta strandi96 – 104Combined sources9
Beta strandi107 – 114Combined sources8
Beta strandi124 – 127Combined sources4
Beta strandi129 – 131Combined sources3
Beta strandi133 – 137Combined sources5
Helixi138 – 140Combined sources3
Beta strandi141 – 146Combined sources6
Beta strandi153 – 155Combined sources3
Beta strandi164 – 167Combined sources4
Turni173 – 175Combined sources3
Helixi188 – 191Combined sources4
Beta strandi205 – 212Combined sources8
Helixi213 – 222Combined sources10
Turni223 – 225Combined sources3
Beta strandi231 – 238Combined sources8
Helixi240 – 252Combined sources13
Beta strandi254 – 256Combined sources3
Beta strandi258 – 261Combined sources4
Beta strandi265 – 271Combined sources7
Helixi276 – 294Combined sources19
Turni295 – 298Combined sources4
Beta strandi301 – 306Combined sources6
Helixi310 – 316Combined sources7
Helixi320 – 322Combined sources3
Helixi335 – 343Combined sources9
Beta strandi354 – 357Combined sources4
Helixi363 – 365Combined sources3
Helixi372 – 376Combined sources5
Helixi387 – 390Combined sources4
Turni391 – 393Combined sources3
Beta strandi400 – 402Combined sources3
Turni410 – 414Combined sources5
Helixi415 – 434Combined sources20
Turni435 – 439Combined sources5
Helixi448 – 464Combined sources17
Helixi469 – 471Combined sources3
Helixi472 – 475Combined sources4
Beta strandi483 – 485Combined sources3
Turni486 – 489Combined sources4
Helixi490 – 496Combined sources7
Turni498 – 501Combined sources4
Helixi504 – 507Combined sources4
Helixi514 – 520Combined sources7
Turni521 – 523Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80B51-529[»]
2F43X-ray3.00B51-529[»]
ProteinModelPortaliP10719.
SMRiP10719.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10719.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP10719.
KOiK02133.
PhylomeDBiP10719.

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.

P10719-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLVGRVAS ASASGALRGL NPLAALPQAH LLLRTAPAGV HPARDYAAQS
60 70 80 90 100
SAAPKAGTAT GQIVAVIGAV VDVQFDEGLP PILNALEVQG RESRLVLEVA
110 120 130 140 150
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE
160 170 180 190 200
PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ 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 AEVFTGHMGK LVPLKETIKG FQQILAGDYD
510 520
HLPEQAFYMV GPIEEAVAKA DKLAEEHGS
Length:529
Mass (Da):56,354
Last modified:April 1, 1990 - v2
Checksum:i9753BFBDBCD30E0F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti257 – 258NL → KV in AAA40778 (PubMed:2907347).Curated2
Sequence conflicti429 – 430QD → HV in AAA40778 (PubMed:2907347).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099743 mRNA. Translation: AAH99743.1.
M25301 mRNA. Translation: AAA57154.1.
M19044 mRNA. Translation: AAB02288.1. Sequence problems.
M57634 mRNA. Translation: AAA40778.1.
PIRiA28701.
A30160.
RefSeqiNP_599191.1. NM_134364.1.
UniGeneiRn.92965.

Genome annotation databases

GeneIDi171374.
KEGGirno:171374.
UCSCiRGD:621368. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099743 mRNA. Translation: AAH99743.1.
M25301 mRNA. Translation: AAA57154.1.
M19044 mRNA. Translation: AAB02288.1. Sequence problems.
M57634 mRNA. Translation: AAA40778.1.
PIRiA28701.
A30160.
RefSeqiNP_599191.1. NM_134364.1.
UniGeneiRn.92965.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80B51-529[»]
2F43X-ray3.00B51-529[»]
ProteinModelPortaliP10719.
SMRiP10719.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251212. 4 interactors.
IntActiP10719. 7 interactors.
MINTiMINT-4587159.
STRINGi10116.ENSRNOP00000003965.

Chemistry databases

ChEMBLiCHEMBL2176796.

PTM databases

iPTMnetiP10719.
PhosphoSitePlusiP10719.

2D gel databases

UCD-2DPAGEP10719.
World-2DPAGE0004:P10719.

Proteomic databases

PaxDbiP10719.
PRIDEiP10719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi171374.
KEGGirno:171374.
UCSCiRGD:621368. rat.

Organism-specific databases

CTDi506.
RGDi621368. Atp5b.

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP10719.
KOiK02133.
PhylomeDBiP10719.

Enzyme and pathway databases

BRENDAi3.6.3.14. 5301.

Miscellaneous databases

EvolutionaryTraceiP10719.
PROiP10719.

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_RAT
AccessioniPrimary (citable) accession number: P10719
Secondary accession number(s): Q499W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds calcium ions.

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.