Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A290DR72 · A0A290DR72_9ASPA

  • Protein
    ATP synthase subunit beta, chloroplastic
  • Gene
    atpB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

149550100150200250300350400450
TypeIDPosition(s)Description
Binding site172-179ATP (UniProtKB | ChEBI)

GO annotations

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
  • Organism
    Hosta minor
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Asparagaceae > Agavoideae > Hosta

Accessions

  • Primary accession
    A0A290DR72

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
    495
  • Mass (Da)
    53,299
  • Last updated
    2017-12-20 v1
  • MD5 Checksum
    5DAB0C1AABE865479EACFF1978DBECCD
MKINPTTSGPAVSTLEEKNLGRIAQIIGPVLDVVFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAALSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEGEKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KX822777
EMBL· GenBank· DDBJ
ATB18925.1
EMBL· GenBank· DDBJ
Genomic DNA
MK732316
EMBL· GenBank· DDBJ
QHF17543.1
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.
Help