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Protein

ATP synthase subunit c

Gene

atpE

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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
Sitei64 – 641Reversibly 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

Enzyme and pathway databases

BioCyciCACE272562:GJIH-2953-MONOMER.

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
Synonyms:atpC
Ordered Locus Names:CA_C2870
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000814 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3421HelicalUniRule annotationAdd
BLAST
Transmembranei60 – 8021HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, CF(0), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8181ATP synthase subunit cPRO_0000112143Add
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 three main subunits: a1, b2 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 and b chains.UniRule annotation

Protein-protein interaction databases

STRINGi272562.CA_C2870.

Structurei

3D structure databases

ProteinModelPortaliO08310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0636. LUCA.
HOGENOMiHOG000235245.
KOiK02110.
OMAiVRGTQEG.
OrthoDBiEOG68H8G3.

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.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
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.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIDSHTFLL GMQYLGAGLA AIGCIGGGVG IGTVTGKAVE AIGRQPESAS
60 70 80
KVMPTMIMGL AFAEVTSLYA LFVAIMLLFV K
Length:81
Mass (Da):8,322
Last modified:July 1, 1997 - v1
Checksum:i0493EFA285ECCABC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52367 Genomic DNA. Translation: AAB50192.1.
AF101055 Genomic DNA. Translation: AAD16421.1.
AE001437 Genomic DNA. Translation: AAK80813.1.
PIRiB97253.
RefSeqiNP_349473.1. NC_003030.1.
WP_010966154.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK80813; AAK80813; CA_C2870.
GeneIDi1119053.
KEGGicac:CA_C2870.
PATRICi32040151. VBICloAce74127_3054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52367 Genomic DNA. Translation: AAB50192.1.
AF101055 Genomic DNA. Translation: AAD16421.1.
AE001437 Genomic DNA. Translation: AAK80813.1.
PIRiB97253.
RefSeqiNP_349473.1. NC_003030.1.
WP_010966154.1. NC_003030.1.

3D structure databases

ProteinModelPortaliO08310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272562.CA_C2870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK80813; AAK80813; CA_C2870.
GeneIDi1119053.
KEGGicac:CA_C2870.
PATRICi32040151. VBICloAce74127_3054.

Phylogenomic databases

eggNOGiCOG0636. LUCA.
HOGENOMiHOG000235245.
KOiK02110.
OMAiVRGTQEG.
OrthoDBiEOG68H8G3.

Enzyme and pathway databases

BioCyciCACE272562:GJIH-2953-MONOMER.

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.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
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.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the F0 structural subunits a, c, and b of the F-type ATP synthases from Clostridium acetobutylicum."
    Belouski E., Bennett G.N.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
  2. "Sequence analysis of the atp operon of Clostridium acetobutylicum DSM 792 encoding the F0F1 ATP synthase."
    Externbrink T., Hujer S., Winzer K., Duerre P.
    DNA Seq. 11:109-118(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Entry informationi

Entry nameiATPL_CLOAB
AccessioniPrimary (citable) accession number: O08310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 1, 1997
Last modified: November 11, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.