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P68699 (ATPL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:atpE
Synonyms:papH, uncE
Ordered Locus Names:b3737, JW3715
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length79 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. HAMAP-Rule MF_01396

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. HAMAP-Rule MF_01396

Subunit structure

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 c10. 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. Ref.12

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.13.

Miscellaneous

Dicyclohexylcarbodiimide (DCDD) binding to the reversibly protonated aspartate residue inhibits ATPase in vitro.

In this organism c-rings of between c8 and c12 can be isolated in vivo following experimental manipulations, however only c8 and c9, in addition to c10, are partially functional (Ref.12).

Sequence similarities

Belongs to the ATPase C chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7979ATP synthase subunit c HAMAP-Rule MF_01396
PRO_0000112144

Regions

Topological domain1 – 1010Periplasmic HAMAP-Rule MF_01396
Transmembrane11 – 3121Helical HAMAP-Rule MF_01396
Topological domain32 – 5221Cytoplasmic HAMAP-Rule MF_01396
Transmembrane53 – 7321Helical HAMAP-Rule MF_01396
Topological domain74 – 796Periplasmic HAMAP-Rule MF_01396

Sites

Site611Reversibly protonated during proton transport

Amino acid modifications

Modified residue11N-formylmethionine By similarity

Experimental info

Mutagenesis231G → D in uncE429; unable to assemble in the membrane. Ref.8
Mutagenesis281I → V in DC1; has a functional F0 as well as F1 part. However, the ATPase activity is inhibited. Ref.7
Mutagenesis311L → F in uncE408 and uncE463; unable to assemble in the membrane. Ref.8
Mutagenesis611D → G in DG 7/1; contains an enzymatically active F1 component, but no functional F0 component. Ref.7
Sequence conflict761F → S in CAA23591. Ref.2

Secondary structure

...... 79
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68699 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0F595A69D8AD1F9E

FASTA798,256
        10         20         30         40         50         60 
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV 

        70 
DAIPMIAVGL GLYVMFAVA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRLWECA. B93732.
RefSeqNP_418193.1. NC_000913.3.
YP_491692.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP68699.
SMRP68699. Positions 1-79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-2198N.
IntActP68699. 3 interactions.
MINTMINT-8087956.
STRING511145.b3737.

Protein family/group databases

TCDB3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

PaxDbP68699.
PRIDEP68699.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76760; AAC76760; b3737.
BAE77551; BAE77551; BAE77551.
GeneID12933605.
948253.
KEGGecj:Y75_p3431.
eco:b3737.
PATRIC32122971. VBIEscCol129921_3861.

Organism-specific databases

EchoBASEEB0100.
EcoGeneEG10102. atpE.

Phylogenomic databases

eggNOGCOG0636.
HOGENOMHOG000235244.
KOK02110.
OMADMLYIAA.
OrthoDBEOG68H8G3.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP68699.

Family and domain databases

Gene3D1.20.20.10. 1 hit.
HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR000454. 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]
PfamPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSPR00124. ATPASEC.
SUPFAMSSF81333. SSF81333. 1 hit.
TIGRFAMsTIGR01260. ATP_synt_c. 1 hit.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP68699.
PROP68699.

Entry information

Entry nameATPL_ECOLI
AccessionPrimary (citable) accession number: P68699
Secondary accession number(s): P00844, Q2M855
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene