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Protein

ATP synthase subunit c

Gene

atpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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.
Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.

Sites

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

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW
  2. proton-transporting ATPase activity, rotational mechanism Source: EcoCyc
  3. proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP synthesis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciEcoCyc:ATPE-MONOMER.
ECOL316407:JW3715-MONOMER.
MetaCyc:ATPE-MONOMER.

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit c
Alternative name(s):
ATP synthase F(0) sector subunit c
Dicyclohexylcarbodiimide-binding protein
F-type ATPase subunit c
Short name:
F-ATPase subunit c
Lipid-binding protein
Gene namesi
Name:atpE
Synonyms:papH, uncE
Ordered Locus Names:b3737, JW3715
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10102. atpE.

Subcellular locationi

Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010Periplasmic
Transmembranei11 – 3121HelicalAdd
BLAST
Topological domaini32 – 5221CytoplasmicAdd
BLAST
Transmembranei53 – 7321HelicalAdd
BLAST
Topological domaini74 – 796Periplasmic

GO - Cellular componenti

  1. integral component of membrane Source: EcoliWiki
  2. plasma membrane Source: UniProtKB-SubCell
  3. proton-transporting ATP synthase complex, coupling factor F(o) Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(0), Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231G → D in uncE429; unable to assemble in the membrane. 1 Publication
Mutagenesisi28 – 281I → V in DC1; has a functional F0 as well as F1 part. However, the ATPase activity is inhibited. 1 Publication
Mutagenesisi31 – 311L → F in uncE408 and uncE463; unable to assemble in the membrane. 1 Publication
Mutagenesisi61 – 611D → G in DG 7/1; contains an enzymatically active F1 component, but no functional F0 component. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7979ATP synthase subunit cPRO_0000112144Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionineBy similarity

Keywords - PTMi

Formylation

Proteomic databases

PaxDbiP68699.
PRIDEiP68699.

Expressioni

Gene expression databases

GenevestigatoriP68699.

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). 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.1 Publication

Protein-protein interaction databases

DIPiDIP-2198N.
IntActiP68699. 3 interactions.
MINTiMINT-8087956.
STRINGi511145.b3737.

Structurei

Secondary structure

1
79
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 3938Combined sources
Beta strandi44 – 463Combined sources
Helixi47 – 7832Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A91NMR-A1-79[»]
1ATYNMR-A1-79[»]
1C0VNMR-A1-79[»]
1C17NMR-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1C99NMR-A1-79[»]
1IJPNMR-A1-79[»]
1J7Fmodel-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1L6TNMR-A1-79[»]
1QO1X-ray3.90K/L/M/N/O/P/Q/R/S/T1-79[»]
4UTQelectron microscopy8.00Z1-79[»]
ProteinModelPortaliP68699.
SMRiP68699. Positions 1-79.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68699.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0636.
HOGENOMiHOG000235244.
InParanoidiP68699.
KOiK02110.
OMAiAIPMITV.
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.

P68699-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR
60 70
TQFFIVMGLV DAIPMIAVGL GLYVMFAVA
Length:79
Mass (Da):8,256
Last modified:July 21, 1986 - v1
Checksum:i0F595A69D8AD1F9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761F → S in CAA23591 (PubMed:6266400).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01594 Genomic DNA. Translation: AAA24732.1.
V00310 Genomic DNA. Translation: CAA23591.1.
M25464 Genomic DNA. Translation: AAA83870.1.
M12214 Genomic DNA. Translation: AAA23668.1.
V00266 Genomic DNA. Translation: CAA23522.1.
V00264 Genomic DNA. Translation: CAA23515.1.
V01506 Genomic DNA. Translation: CAA24752.1.
X01631 Genomic DNA. Translation: CAA25777.1.
L10328 Genomic DNA. Translation: AAA62089.1.
U00096 Genomic DNA. Translation: AAC76760.1.
AP009048 Genomic DNA. Translation: BAE77551.1.
PIRiB93732. LWECA.
RefSeqiNP_418193.1. NC_000913.3.
YP_491692.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76760; AAC76760; b3737.
BAE77551; BAE77551; BAE77551.
GeneIDi12933605.
948253.
KEGGiecj:Y75_p3431.
eco:b3737.
PATRICi32122971. VBIEscCol129921_3861.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01594 Genomic DNA. Translation: AAA24732.1.
V00310 Genomic DNA. Translation: CAA23591.1.
M25464 Genomic DNA. Translation: AAA83870.1.
M12214 Genomic DNA. Translation: AAA23668.1.
V00266 Genomic DNA. Translation: CAA23522.1.
V00264 Genomic DNA. Translation: CAA23515.1.
V01506 Genomic DNA. Translation: CAA24752.1.
X01631 Genomic DNA. Translation: CAA25777.1.
L10328 Genomic DNA. Translation: AAA62089.1.
U00096 Genomic DNA. Translation: AAC76760.1.
AP009048 Genomic DNA. Translation: BAE77551.1.
PIRiB93732. LWECA.
RefSeqiNP_418193.1. NC_000913.3.
YP_491692.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A91NMR-A1-79[»]
1ATYNMR-A1-79[»]
1C0VNMR-A1-79[»]
1C17NMR-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1C99NMR-A1-79[»]
1IJPNMR-A1-79[»]
1J7Fmodel-A/B/C/D/E/F/G/H/I/J/K/L1-79[»]
1L6TNMR-A1-79[»]
1QO1X-ray3.90K/L/M/N/O/P/Q/R/S/T1-79[»]
4UTQelectron microscopy8.00Z1-79[»]
ProteinModelPortaliP68699.
SMRiP68699. Positions 1-79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-2198N.
IntActiP68699. 3 interactions.
MINTiMINT-8087956.
STRINGi511145.b3737.

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

PaxDbiP68699.
PRIDEiP68699.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76760; AAC76760; b3737.
BAE77551; BAE77551; BAE77551.
GeneIDi12933605.
948253.
KEGGiecj:Y75_p3431.
eco:b3737.
PATRICi32122971. VBIEscCol129921_3861.

Organism-specific databases

EchoBASEiEB0100.
EcoGeneiEG10102. atpE.

Phylogenomic databases

eggNOGiCOG0636.
HOGENOMiHOG000235244.
InParanoidiP68699.
KOiK02110.
OMAiAIPMITV.
OrthoDBiEOG68H8G3.

Enzyme and pathway databases

BioCyciEcoCyc:ATPE-MONOMER.
ECOL316407:JW3715-MONOMER.
MetaCyc:ATPE-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP68699.
PROiP68699.

Gene expression databases

GenevestigatoriP68699.

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. "Amino acid sequence of the ATPase proteolipid from mitochondria, chloroplasts and bacteria (wild type and mutants)."
    Sebald W., Hoppe J., Wachter E.
    (In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.); Function and molecular aspects of biomembrane transport, pp.63-74, Elsevier, Amsterdam (1979)
    Cited for: PROTEIN SEQUENCE.
  2. "Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-binding protein and the alpha subunit of proton-translocating ATPase of Escherichia coli."
    Kanazawa H., Mabuchi K., Kayano T., Tamura F., Futai M.
    Biochem. Biophys. Res. Commun. 100:219-225(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli."
    Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.
    Mol. Gen. Genet. 184:33-39(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase."
    Gay N.J., Walker J.E.
    Nucleic Acids Res. 9:3919-3926(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation."
    Fimmel A.L., Jans D.A., Langman L., James L.B., Ash G.R., Downie J.A., Senior A.E., Gibson F., Cox G.B.
    Biochem. J. 213:451-458(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
    Walker J.E., Gay N.J., Saraste M., Eberle A.N.
    Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains of Escherichia coli defective in the energy-transducing ATPase complex."
    Wachter E., Schmid R., Deckers G., Altendorf K.
    FEBS Lett. 113:265-270(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, MUTAGENESIS OF ILE-28 AND ASP-61.
    Strain: K12.
  8. "Mutations in the uncE gene affecting assembly of the c-subunit of the adenosine triphosphatase of Escherichia coli."
    Jans D.A., Fimmel A.L., Langman L., James L.B., Downie J.A., Senior A.E., Ash G.R., Gibson F., Cox G.B.
    Biochem. J. 211:717-726(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-23 AND LEU-31.
  9. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  11. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  12. "The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10."
    Jiang W., Hermolin J., Fillingame R.H.
    Proc. Natl. Acad. Sci. U.S.A. 98:4966-4971(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBUNIT C FUSIONS.
  13. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  14. "Heteronuclear 1H-15N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F1F0 ATP synthase: assignment and secondary structure."
    Norwood T.J., Crawford D.A., Steventon M.E., Driscoll P.C., Campbell I.D.
    Biochemistry 31:6285-6290(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SITE.
  15. "Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase."
    Girvin M.E., Fillingame R.H.
    Biochemistry 34:1635-1645(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  16. "Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase."
    Girvin M.E., Rastogi V.K., Abildgaard F., Markley J.L., Fillingame R.H.
    Biochemistry 37:8817-8824(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  17. "Structural changes linked to proton translocation by subunit c of the ATP synthase."
    Rastogi V.K., Girvin M.E.
    Nature 402:263-268(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  18. "Model of the c-subunit oligomer in the membrane domain of F-ATPases."
    Groth G., Walker J.E.
    FEBS Lett. 410:117-123(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiATPL_ECOLI
AccessioniPrimary (citable) accession number: P68699
Secondary accession number(s): P00844, Q2M855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Dicyclohexylcarbodiimide (DCDD) binding to the reversibly protonated aspartate residue inhibits ATPase in vitro.
In this organism c-rings of between c8 and c(12) can be isolated in vivo following experimental manipulations, however only c8 and c9, in addition to c(10), are partially functional.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.