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Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5F1B

Organism
Gallus gallus (Chicken)
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.

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi211 – 218ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • ATP synthesis coupled proton transport Source: InterPro

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrialCurated (EC:3.6.3.14)
Alternative name(s):
ATP synthase F1 subunit betaBy similarity
Gene namesi
Name:ATP5F1BBy similarity
Synonyms:ATP5BBy similarity
ORF Names:RCJMB04_6l18
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53MitochondrionBy similarityAdd BLAST53
ChainiPRO_000022350154 – 533ATP synthase subunit beta, mitochondrialAdd BLAST480

Proteomic databases

PaxDbiQ5ZLC5
PRIDEiQ5ZLC5

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.Curated

Protein-protein interaction databases

BioGridi686196, 2 interactors
IntActiQ5ZLC5, 1 interactor
STRINGi9031.ENSGALP00000035339

Structurei

3D structure databases

ProteinModelPortaliQ5ZLC5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Sequence analysis

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350 Eukaryota
COG0055 LUCA
HOGENOMiHOG000009605
HOVERGENiHBG004307
InParanoidiQ5ZLC5
KOiK02133
PhylomeDBiQ5ZLC5

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.

Q5ZLC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGLAGRCSA AAASAARPAL RRAAGPSHGF LPLLLSRGAG PAAAVGARRD
60 70 80 90 100
HAAQAAPAAK AGSATGRIVA VIGAVVDVQF DEGLPPILNA LEVQGRETRL
110 120 130 140 150
VLEVAQHLGE NTVRTIAMDG TEGLVRGQKV LDSGAPIRIP VGPETLGRIM
160 170 180 190 200
NVIGEPIDER GPITTKQFAA IHAEAPEFVE MSVEQKILVT GIKVVDLLAP
210 220 230 240 250
YAKGGKIGLF GGAGVGKTVL IMELINNVAK AHGGYSVFAG VGERTREGND
260 270 280 290 300
LYHEMIESGV INLKDATSKV ALVYGQMNEP PGARARVALT GLTVAEYFRD
310 320 330 340 350
QEGQDVLLFI DNIFRFTQAG SEVSALLGRI PSAVGYQPTL ATDMGTMQER
360 370 380 390 400
ITTTRKGSIT SVQAIYVPAD DLTDPAPATT FAHLDATTVL SRAIAELGIY
410 420 430 440 450
PAVDPLDSTS RIMDPNIVGP EHYDVARGVQ KILQDYKSLQ DIIAILGMDE
460 470 480 490 500
LSEEDKLTVA RARKIQRFLS QPFQVAEVFT GHMGKLVPLK ETIKGFKQIL
510 520 530
AGEYDHLPEQ AFYMVGPIEE AVAKAEKLAE EHA
Length:533
Mass (Da):56,628
Last modified:November 23, 2004 - v1
Checksum:i84C9945D1AAD8832
GO

Mass spectrometryi

Molecular mass is 51171±1 Da from positions 54 - 533. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ719809 mRNA Translation: CAG31468.1
RefSeqiNP_001026562.2, NM_001031391.2
UniGeneiGga.22609
Gga.44379

Genome annotation databases

GeneIDi426673
KEGGigga:426673

Similar proteinsi

Entry informationi

Entry nameiATPB_CHICK
AccessioniPrimary (citable) accession number: Q5ZLC5
Secondary accession number(s): P84168
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 23, 2004
Last modified: March 28, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health