P49647 · ATPB_TRICV

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.

147550100150200250300350400450
TypeIDPosition(s)Description
Binding site156-163ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother 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

Accessions

  • Primary accession
    P49647

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001445341-475ATP synthase subunit beta, chloroplastic

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).

Structure

Family & Domains

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    475
  • Mass (Da)
    51,509
  • Last updated
    1996-02-01 v1
  • Checksum
    5BDA89DAA9D4DA2C
MVKTNINKGYVNQIIGPVLDIEFPSGTLPPIYSALKIETEDGIGTVVEVQQLLGDNKVRAVSMRSTDGLKRGVEARDLGGPISVPVGISTLGRIFNVIGEPVDEQGDVSYDETLPIHREAPAFTELETKPSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYEEMKESGVINENNFKESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTTQGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLDSTSTMLQPGIVSGEHYEIAETVKETLQRYKELQDIIAILGIDELSEEDRLTVARARKVERFLSQPFFVAEIFTGSPGKYVSLEETIKGFTMVLKGELDELPEQAFYLVGNIDEAIAKAETLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X72497
EMBL· GenBank· DDBJ
CAA51161.1
EMBL· GenBank· DDBJ
Genomic DNA
Z67753
EMBL· GenBank· DDBJ
CAA91739.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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