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Protein

ATP synthase subunit a

Gene

atpB

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

Functioni

Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit aUniRule annotation
Alternative name(s):
ATP synthase F0 sector subunit aUniRule annotation
F-ATPase subunit 6UniRule annotation
Gene namesi
Name:atpBUniRule 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
Transmembranei18 – 3821HelicalUniRule annotationAdd
BLAST
Transmembranei77 – 9721HelicalUniRule annotationAdd
BLAST
Transmembranei103 – 12321HelicalUniRule annotationAdd
BLAST
Transmembranei132 – 15221HelicalUniRule annotationAdd
BLAST
Transmembranei185 – 20521HelicalUniRule annotationAdd
BLAST
Transmembranei209 – 22921HelicalUniRule 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 – 237237ATP synthase subunit aPRO_0000239035Add
BLAST

Interactioni

Subunit structurei

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.UniRule annotation

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00741.

Structurei

3D structure databases

ProteinModelPortaliO05330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase A chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EE4. Bacteria.
COG0356. LUCA.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
HAMAPiMF_01393. ATP_synth_a_bact.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O05330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDGEAIRWF EFFVPTNSTL WMAIGVLMIA LLMVVGTLRR AIVPGRIQSL
60 70 80 90 100
AELTYGFIHK MVEDVAGKDG LVYFPYIFTL FLFILFSNFL GLIPMAFTPT
110 120 130 140 150
SHIAVTGVMA MGVFIGVTAL GFMKHGSHFL NLFWVSAAPL PLRPILAVIE
160 170 180 190 200
VISYFVRPVS HSIRLAGNMM AGHAVMEVFA AFAPLILFSF VGVIVTPLSV
210 220 230
LAIVAMYALE ILVAFVQAYV FTILTCVYLK DALHPGH
Length:237
Mass (Da):26,096
Last modified:July 1, 1997 - v1
Checksum:iCB623F47295F4862
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12313 Genomic DNA. Translation: CAA72981.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12313 Genomic DNA. Translation: CAA72981.1.

3D structure databases

ProteinModelPortaliO05330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00741.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105EE4. Bacteria.
COG0356. LUCA.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
HAMAPiMF_01393. ATP_synth_a_bact.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]
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 nameiATP6_RHOCA
AccessioniPrimary (citable) accession number: O05330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 1, 1997
Last modified: November 11, 2015
This is version 77 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.