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P0A6E6

- ATPE_ECOLI

UniProt

P0A6E6 - ATPE_ECOLI

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Protein

ATP synthase epsilon chain

Gene

atpC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane.

GO - Molecular functioni

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

GO - Biological processi

  1. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:ATPC-MONOMER.
ECOL316407:JW3709-MONOMER.
MetaCyc:ATPC-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 epsilon chain
Alternative name(s):
ATP synthase F1 sector epsilon subunit
F-ATPase epsilon subunit
Gene namesi
Name:atpC
Synonyms:papG, uncC
Ordered Locus Names:b3731, JW3709
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10100. atpC.

Subcellular locationi

Cell inner membrane 2 Publications; Peripheral membrane protein 2 Publications

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-HAMAP
  2. proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 139138ATP synthase epsilon chainPRO_0000188132Add
BLAST

Proteomic databases

PaxDbiP0A6E6.
PRIDEiP0A6E6.

2D gel databases

SWISS-2DPAGEP0A6E6.

Expressioni

Gene expression databases

GenevestigatoriP0A6E6.

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: a, b and c.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
atpGP0ABA64EBI-544362,EBI-544306

Protein-protein interaction databases

DIPiDIP-47828N.
IntActiP0A6E6. 7 interactions.
STRINGi511145.b3731.

Structurei

Secondary structure

1
139
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Beta strandi15 – 3521Combined sources
Beta strandi42 – 465Combined sources
Beta strandi48 – 558Combined sources
Turni56 – 583Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 725Combined sources
Beta strandi77 – 815Combined sources
Helixi88 – 10316Combined sources
Beta strandi110 – 1123Combined sources
Helixi115 – 13319Combined sources
Helixi134 – 1374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A6E6.
SMRiP0A6E6. Positions 2-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6E6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase epsilon chain family.Curated

Phylogenomic databases

eggNOGiCOG0355.
HOGENOMiHOG000216025.
InParanoidiP0A6E6.
KOiK02114.
OMAiHIFNGEV.
OrthoDBiEOG690MN9.
PhylomeDBiP0A6E6.

Family and domain databases

Gene3Di2.60.15.10. 1 hit.
HAMAPiMF_00530. ATP_synth_epsil_bac.
InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
IPR020547. ATPase_F1_dsu/esu_C.
[Graphical view]
PANTHERiPTHR13822. PTHR13822. 1 hit.
PfamiPF00401. ATP-synt_DE. 1 hit.
PF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46604. SSF46604. 1 hit.
SSF51344. SSF51344. 1 hit.
TIGRFAMsiTIGR01216. ATP_synt_epsi. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6E6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMTYHLDVV SAEQQMFSGL VEKIQVTGSE GELGIYPGHA PLLTAIKPGM
60 70 80 90 100
IRIVKQHGHE EFIYLSGGIL EVQPGNVTVL ADTAIRGQDL DEARAMEAKR
110 120 130
KAEEHISSSH GDVDYAQASA ELAKAIAQLR VIELTKKAM
Length:139
Mass (Da):15,068
Last modified:January 23, 2007 - v2
Checksum:i5EFF7DE911745A62
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131E → K AA sequence (PubMed:9868784)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB90106. PWECE.
RefSeqiNP_418187.1. NC_000913.3.
YP_491698.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76754; AAC76754; b3731.
BAE77557; BAE77557; BAE77557.
GeneIDi12932183.
948245.
KEGGiecj:Y75_p3437.
eco:b3731.
PATRICi32122959. VBIEscCol129921_3855.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi B90106. PWECE.
RefSeqi NP_418187.1. NC_000913.3.
YP_491698.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AQT X-ray 2.30 A 4-139 [» ]
1BSH NMR - A 2-139 [» ]
1BSN NMR - A 2-139 [» ]
1FS0 X-ray 2.10 E 2-139 [» ]
1QO1 X-ray 3.90 J 4-139 [» ]
3OAA X-ray 3.26 H/P/X/f 2-139 [» ]
ProteinModelPortali P0A6E6.
SMRi P0A6E6. Positions 2-139.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47828N.
IntActi P0A6E6. 7 interactions.
STRINGi 511145.b3731.

Protein family/group databases

TCDBi 3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGE P0A6E6.

Proteomic databases

PaxDbi P0A6E6.
PRIDEi P0A6E6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76754 ; AAC76754 ; b3731 .
BAE77557 ; BAE77557 ; BAE77557 .
GeneIDi 12932183.
948245.
KEGGi ecj:Y75_p3437.
eco:b3731.
PATRICi 32122959. VBIEscCol129921_3855.

Organism-specific databases

EchoBASEi EB0098.
EcoGenei EG10100. atpC.

Phylogenomic databases

eggNOGi COG0355.
HOGENOMi HOG000216025.
InParanoidi P0A6E6.
KOi K02114.
OMAi HIFNGEV.
OrthoDBi EOG690MN9.
PhylomeDBi P0A6E6.

Enzyme and pathway databases

BioCyci EcoCyc:ATPC-MONOMER.
ECOL316407:JW3709-MONOMER.
MetaCyc:ATPC-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6E6.
PROi P0A6E6.

Gene expression databases

Genevestigatori P0A6E6.

Family and domain databases

Gene3Di 2.60.15.10. 1 hit.
HAMAPi MF_00530. ATP_synth_epsil_bac.
InterProi IPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
IPR020547. ATPase_F1_dsu/esu_C.
[Graphical view ]
PANTHERi PTHR13822. PTHR13822. 1 hit.
Pfami PF00401. ATP-synt_DE. 1 hit.
PF02823. ATP-synt_DE_N. 1 hit.
[Graphical view ]
ProDomi PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF46604. SSF46604. 1 hit.
SSF51344. SSF51344. 1 hit.
TIGRFAMsi TIGR01216. ATP_synt_epsi. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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).

Entry informationi

Entry nameiATPE_ECOLI
AccessioniPrimary (citable) accession number: P0A6E6
Secondary accession number(s): P00832, Q2M849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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