A0A7L7T4D3 · A0A7L7T4D3_PRUDO

Function

function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site172-179ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchloroplast thylakoid membrane
Cellular Componentproton-transporting ATP synthase complex, catalytic core F(1)
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionproton-transporting ATP synthase activity, rotational mechanism
Molecular Functionproton-transporting ATPase activity, rotational mechanism

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP synthase subunit beta, chloroplastic
  • EC number
  • Alternative names
    • ATP synthase F1 sector subunit beta
    • F-ATPase subunit beta

Gene names

    • Name
      atpB

Encoded on

  • Chloroplast

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus

Accessions

  • Primary accession
    A0A7L7T4D3

Subcellular Location

Keywords

Interaction

Subunit

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 four main subunits: a1, b1, b'1 and c(9-12).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain164-356AAA+ ATPase

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    492
  • Mass (Da)
    52,830
  • Last updated
    2021-04-07 v1
  • Checksum
    A4ABD14A349D4099
MRINPTTSGPGVPALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVRGRDAVGQQINVTCEVQQLLGNNRVRAVAMSATDGLKRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKETLQRYKELQDIIAILGLDELSEDDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELDGLPEQAFYLVGNIDEATAKATTLGT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MT302569
EMBL· GenBank· DDBJ
QOC70456.1
EMBL· GenBank· DDBJ
Genomic DNA
MW406464
EMBL· GenBank· DDBJ
QWK45895.1
EMBL· GenBank· DDBJ
Genomic DNA
MW406471
EMBL· GenBank· DDBJ
QWK46490.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp