A0A1B1W4S3 · A0A1B1W4S3_ARATH

Function

function

F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.
This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase.

Miscellaneous

In plastids the F-type ATPase is also known as CF1CF0.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for site.

TypeIDPosition(s)Description
Site61Reversibly protonated during proton transport

GO annotations

AspectTerm
Cellular Componentchloroplast thylakoid membrane
Cellular Componentproton-transporting ATP synthase complex, coupling factor F(o)
Molecular Functionlipid binding
Molecular Functionproton-transporting ATP synthase activity, rotational mechanism

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    ATP synthase subunit c, chloroplastic
  • Alternative names
    • ATP synthase F(0) sector subunit c
    • ATPase subunit III
    • F-type ATPase subunit c
      (F-ATPase subunit c
      )
    • Lipid-binding protein

Gene names

    • Name
      atpH

Encoded on

  • Chloroplast

Organism names

  • Taxonomic identifier
  • Strain
    • 180404IB4
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    A0A1B1W4S3

Organism-specific databases

Genome annotation databases

Subcellular Location

Membrane
; Multi-pass membrane protein
Plastid, chloroplast thylakoid membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane57-77Helical

Keywords

Expression

Gene expression databases

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: a, b and c.
F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has four main subunits: a1, b1, b'1 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-73V-ATPase proteolipid subunit C-like

Sequence similarities

Belongs to the ATPase C chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    81
  • Mass (Da)
    7,976
  • Last updated
    2016-11-02 v1
  • Checksum
    2EA40BC2265B3CB9
MNPLVSAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KX551970
EMBL· GenBank· DDBJ
ANW47777.1
EMBL· GenBank· DDBJ
Genomic DNA
MK353213
EMBL· GenBank· DDBJ
QBI37850.1
EMBL· GenBank· DDBJ
Genomic DNA
MK380719
EMBL· GenBank· DDBJ
QDK58742.1
EMBL· GenBank· DDBJ
Genomic DNA
MK380720
EMBL· GenBank· DDBJ
QDK58827.1
EMBL· GenBank· DDBJ
Genomic DNA
MK380721
EMBL· GenBank· DDBJ
QDK58912.1
EMBL· GenBank· DDBJ
Genomic DNA
MN603471
EMBL· GenBank· DDBJ
QXM16418.1
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