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P0A6E6 (ATPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase epsilon chain
Alternative name(s):
ATP synthase F1 sector epsilon subunit
F-ATPase epsilon subunit
Gene names
Name:atpC
Synonyms:papG, uncC
Ordered Locus Names:b3731, JW3709
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. HAMAP-Rule MF_00530

Subunit structure

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: a, b and c. Ref.10

Subcellular location

Cell inner membrane; Peripheral membrane protein Ref.10 Ref.11.

Sequence similarities

Belongs to the ATPase epsilon chain family.

Sequence caution

The sequence CAA23528.1 differs from that shown. Reason: Frameshift at position 132.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

atpGP0ABA64EBI-544362,EBI-544306

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 139138ATP synthase epsilon chain HAMAP-Rule MF_00530
PRO_0000188132

Experimental info

Sequence conflict131E → K AA sequence Ref.8

Secondary structure

....................... 139
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6E6 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5EFF7DE911745A62

FASTA13915,068
        10         20         30         40         50         60 
MAMTYHLDVV SAEQQMFSGL VEKIQVTGSE GELGIYPGHA PLLTAIKPGM IRIVKQHGHE 

        70         80         90        100        110        120 
EFIYLSGGIL EVQPGNVTVL ADTAIRGQDL DEARAMEAKR KAEEHISSSH GDVDYAQASA 

       130 
ELAKAIAQLR VIELTKKAM 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"Nucleotide sequence of the genes for beta and epsilon subunits of proton-translocating ATPase from Escherichia coli."
Kanazawa H., Kayano T., Kiyasu T., Futai M.
Biochem. Biophys. Res. Commun. 105:1257-1264(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase."
Kanazawa H., Futai M.
Ann. N. Y. Acad. Sci. 402:45-64(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase."
Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.
Nucleic Acids Res. 9:5287-5296(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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.
[6]"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.
[7]"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.
[8]"Small genes/gene-products in Escherichia coli K-12."
Wasinger V.C., Humphery-Smith I.
FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Strain: K12.
[9]Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
Submitted (FEB-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-9.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[11]"Membrane localization of small proteins in Escherichia coli."
Fontaine F., Fuchs R.T., Storz G.
J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[12]"Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy."
Wilkens S., Dahlquist F.W., McIntosh L.P., Donaldson L.W., Capaldi R.A.
Nat. Struct. Biol. 2:961-967(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[13]"Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex."
Wilkens S., Capaldi R.A.
J. Biol. Chem. 273:26645-26651(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[14]"Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli."
Uhlin U., Cox G.B., Guss J.M.
Structure 5:1219-1230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01594 Genomic DNA. Translation: AAA24738.1.
X01631 Genomic DNA. Translation: CAA25783.1.
V00311 Genomic DNA. Translation: CAA23595.1.
M25464 Genomic DNA. Translation: AAA83876.1.
V00267 Genomic DNA. Translation: CAA23528.1. Frameshift.
L10328 Genomic DNA. Translation: AAA62083.1.
U00096 Genomic DNA. Translation: AAC76754.1.
AP009048 Genomic DNA. Translation: BAE77557.1.
PIRPWECE. B90106.
RefSeqNP_418187.1. NC_000913.3.
YP_491698.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQTX-ray2.30A4-139[»]
1BSHNMR-A2-139[»]
1BSNNMR-A2-139[»]
1FS0X-ray2.10E2-139[»]
1QO1X-ray3.90J4-139[»]
3OAAX-ray3.26H/P/X/f2-139[»]
ProteinModelPortalP0A6E6.
SMRP0A6E6. Positions 2-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47828N.
IntActP0A6E6. 7 interactions.
STRING511145.b3731.

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.

2D gel databases

SWISS-2DPAGEP0A6E6.

Proteomic databases

PaxDbP0A6E6.
PRIDEP0A6E6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76754; AAC76754; b3731.
BAE77557; BAE77557; BAE77557.
GeneID12932183.
948245.
KEGGecj:Y75_p3437.
eco:b3731.
PATRIC32122959. VBIEscCol129921_3855.

Organism-specific databases

EchoBASEEB0098.
EcoGeneEG10100. atpC.

Phylogenomic databases

eggNOGCOG0355.
HOGENOMHOG000216025.
KOK02114.
OMAHIFNGEV.
OrthoDBEOG690MN9.
PhylomeDBP0A6E6.

Enzyme and pathway databases

BioCycEcoCyc:ATPC-MONOMER.
ECOL316407:JW3709-MONOMER.
MetaCyc:ATPC-MONOMER.

Gene expression databases

GenevestigatorP0A6E6.

Family and domain databases

Gene3D2.60.15.10. 1 hit.
HAMAPMF_00530. ATP_synth_epsil_bac.
InterProIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
IPR020547. ATPase_F1_dsu/esu_C.
[Graphical view]
PANTHERPTHR13822. PTHR13822. 1 hit.
PfamPF00401. ATP-synt_DE. 1 hit.
PF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF46604. SSF46604. 1 hit.
SSF51344. SSF51344. 1 hit.
TIGRFAMsTIGR01216. ATP_synt_epsi. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A6E6.
PROP0A6E6.

Entry information

Entry nameATPE_ECOLI
AccessionPrimary (citable) accession number: P0A6E6
Secondary accession number(s): P00832, Q2M849
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 2 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