A5HY52 · ATPB_CLOBH

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.

146350100150200250300350400450
TypeIDPosition(s)Description
Binding site151-158ATP (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 Componentplasma 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
  • EC number
  • Alternative names
    • ATP synthase F1 sector subunit beta
    • F-ATPase subunit beta

Gene names

    • Name
      atpD
    • Ordered locus names
      CBO0156, CLC_0204

Organism names

Accessions

  • Primary accession
    A5HY52
  • Secondary accessions
    • A7G072

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003395171-463ATP synthase subunit beta

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 three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.

Structure

Family & Domains

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    463
  • Mass (Da)
    50,787
  • Last updated
    2007-06-26 v1
  • Checksum
    D074814B7B9D0503
MSNLGKVIQIIGPIIDIKFDSENLPDLFNALEINAGDRKVIAEVEQHIGDDTIRAIAMEDTEGLKRGMEALDTGKSVSVPVGKEVLGRLFNVLGKPIDGAGEFISEESYPIHRPAPSFEEQSVEPEIFETGIKVIDLLAPYQKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGLSVFTGVGERTREGNDLYYEMKESGVLEKTALVFGQMNEPPGARMRVALTGLTMSEYFRDQGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGALQERITSTKNGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSITELGIYPAVDPLESSSRMLDPRIIGEEHYEVAIKVKNILERYRELQDIIAILGIDELSEEDKLVVGRARKIQRFLSQPFTVAEQFTGMQGKYVPIKETVRGFKEILEGKHDNIPESAFLFQGTIEDVLKKAQQMEI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000727
EMBL· GenBank· DDBJ
ABS37210.1
EMBL· GenBank· DDBJ
Genomic DNA
AM412317
EMBL· GenBank· DDBJ
CAL81711.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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