ATP synthase epsilon chain - Escherichia coli (strain K12)

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P0A6E6 (ATPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the ATPase epsilon chain family.
Sequence caution	The sequence CAA23528.1 differs from that shown. Reason: Frameshift at position 132.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from direct assay PubMed 6238948. Source: EcoliWiki
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP proton-transporting ATP synthase activity, rotational mechanism Inferred from direct assay PubMed 6238948. Source: EcoCyc proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.8 Ref.9

Chain

2 – 139

138

ATP synthase epsilon chain HAMAP-Rule MF_00530

PRO_0000188132

Experimental info

Sequence conflict

E → K AA sequence Ref.8

Secondary structure

139

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6E6 [UniParc].

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

139

15,068

        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' referencesShow '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 277:1453-1474(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]	"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.
[12]	"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.
[13]	"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.

PIR

PWECE. B90106.

RefSeq

NP_418187.1. NC_000913.2.
YP_491698.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-138	[»]
1QO1	X-ray	3.90	J	4-139	[»]
3OAA	X-ray	3.26	H/P/X/f	2-139	[»]

ProteinModelPortal

P0A6E6.

SMR

P0A6E6. Positions 2-139.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47828N.

IntAct

P0A6E6. 4 interactions.

STRING

511145.b3731.

Protein family/group databases

TCDB

3.A.2.1.1. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

2D gel databases

SWISS-2DPAGE

P0A6E6.

Proteomic databases

PaxDb

P0A6E6.

PRIDE

P0A6E6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76754; AAC76754; b3731.
BAE77557; BAE77557; BAE77557.

GeneID

12932183.
948245.

KEGG

ecj:Y75_p3437.
eco:b3731.

PATRIC

32122959. VBIEscCol129921_3855.

Organism-specific databases

EchoBASE

EB0098.

EcoGene

EG10100. atpC.

Phylogenomic databases

eggNOG

COG0355.

HOGENOM

HOG000216025.

K02114.

OMA

SAEASIF.

ProtClustDB

PRK00571.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A6E6.

Family and domain databases

Gene3D

2.60.15.10. 1 hit.

HAMAP

MF_00530. ATP_synth_epsil_bac.

InterPro

IPR001469. ATPase_F1-cplx_dsu/esu.
IPR020547. ATPase_F1-cplx_dsu/esu_C.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
[Graphical view]

PANTHER

PTHR13822. PTHR13822. 1 hit.

Pfam

PF00401. ATP-synt_DE. 1 hit.
PF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]

ProDom

PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF46604. ATPsynt_DE. 1 hit.
SSF51344. ATPsynt_DE. 1 hit.

TIGRFAMs

TIGR01216. ATP_synt_epsi. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6E6.

Entry information

Entry name

ATPE_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents