Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP synthase subunit c

Gene

atpE

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation
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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei61 – 611Reversibly protonated during proton transportUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit cUniRule annotation
Alternative name(s):
ATP synthase F(0) sector subunit cUniRule annotation
F-type ATPase subunit cUniRule annotation
Short name:
F-ATPase subunit cUniRule annotation
Lipid-binding proteinUniRule annotation
Gene namesi
Name:atpEUniRule annotation
OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifieri1061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Subcellular locationi

  • Cellular chromatophore membrane 1 Publication; Multi-pass membrane protein UniRule annotation1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221HelicalUniRule annotationAdd
BLAST
Transmembranei54 – 7421HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7878ATP synthase subunit cPRO_0000239039Add
BLAST

Interactioni

Subunit structurei

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.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00742.

Structurei

3D structure databases

ProteinModelPortaliO05331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105VD1. Bacteria.
ENOG41121M2. LUCA.
HOGENOMiHOG000235245.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.

Sequencei

Sequence statusi: Complete.

O05331-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGDIVQMGA YIGAGLACTG MGGAAVGVGH VVGNFISGAL RNPSAAASQT
60 70
ATMFIGIAFA EALGIFSFLV ALLLMFAV
Length:78
Mass (Da):7,696
Last modified:July 1, 1997 - v1
Checksum:iA7D265332A39D6C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12313 Genomic DNA. Translation: CAA72982.1.
RefSeqiWP_013066486.1. NZ_LLVV01000017.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12313 Genomic DNA. Translation: CAA72982.1.
RefSeqiWP_013066486.1. NZ_LLVV01000017.1.

3D structure databases

ProteinModelPortaliO05331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105VD1. Bacteria.
ENOG41121M2. LUCA.
HOGENOMiHOG000235245.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR002379. ATPase_proteolipid_c-like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
TIGRFAMsiTIGR01260. ATP_synt_c. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The atpIBEXF operon coding for the Fo sector of the ATP synthase from the purple nonsulfur photosynthetic bacterium Rhodobacter capsulatus."
    Borghese R., Turina P., Lambertini L., Melandri B.A.
    Arch. Microbiol. 170:385-388(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33303 / B10.
  2. "Purification of the H+-ATPase from Rhodobacter capsulatus, identification of the F1F0 components and reconstitution of the active enzyme."
    Gabellini N., Gao Z., Eckerskorn C., Lottspeich F., Oesterhelt D.
    Biochim. Biophys. Acta 934:227-234(1988)
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: GA.

Entry informationi

Entry nameiATPL_RHOCA
AccessioniPrimary (citable) accession number: O05331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 1, 1997
Last modified: January 20, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.