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Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5B

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 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).Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 2188ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • ATP hydrolysis coupled proton transport Source: InterPro
  • ATP synthesis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353MitochondrionBy similarityAdd
BLAST
Chaini54 – 533480ATP synthase subunit beta, mitochondrialPRO_0000223501Add
BLAST

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 interactions.
IntActiQ5ZLC5. 1 interaction.
STRINGi9031.ENSGALP00000035339.

Structurei

3D structure databases

ProteinModelPortaliQ5ZLC5.
SMRiQ5ZLC5. Positions 65-532.
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.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_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]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. 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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ5ZLC5.
SMRiQ5ZLC5. Positions 65-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi686196. 2 interactions.
IntActiQ5ZLC5. 1 interaction.
STRINGi9031.ENSGALP00000035339.

Proteomic databases

PaxDbiQ5ZLC5.
PRIDEiQ5ZLC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi426673.
KEGGigga:426673.

Organism-specific databases

CTDi506.

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiQ5ZLC5.
KOiK02133.
PhylomeDBiQ5ZLC5.

Miscellaneous databases

PROiQ5ZLC5.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_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]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: CBImported.
    Tissue: Bursa of FabriciusImported.
  2. "Proteomic analysis of the Gallus gallus embryo at stage-29 of development."
    Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J., Schneider J., Palomar M.A., Linares R.
    Proteomics 5:4946-4957(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, MASS SPECTROMETRY.
    Tissue: Embryo1 Publication.

Entry informationi

Entry nameiATPB_CHICK
AccessioniPrimary (citable) accession number: Q5ZLC5
Secondary accession number(s): P84168
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 23, 2004
Last modified: June 8, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.