Reviewed, UniProtKB/Swiss-Prot P0A6E6 (ATPE_ECOLI)

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) [Complete 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 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
Gene Ontology (GO)
Biological process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP 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

1

1

Removed Ref.8 Ref.9

Chain

2 – 139

138

ATP synthase epsilon chain HAMAP MF_00530

PRO_0000188132

Experimental info

Sequence conflict

13

1

E → K AA sequence Ref.8

Secondary structure

1

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139

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Beta strand

15 – 35

21

Beta strand

42 – 46

5

Beta strand

48 – 55

8

Turn

56 – 58

3

Beta strand

59 – 73

15

Beta strand

76 – 86

11

Helix

87 – 89

3

Helix

92 – 106

15

Beta strand

110 – 112

3

Helix

113 – 136

24

Sequences

	Sequence		Length	Mass (Da)
	P0A6E6-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5EFF7DE911745A62	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

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: 6395859] [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: 6285901] [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: 6301339] [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: 6272217] [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: 7686882] [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: 9278503] [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: 16738553] [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: 9868784] [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: 16079137] [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: 7583669] [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: 9756905] [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: 9331422] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_004056.1.
NP_418187.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A6E6.

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.

2-D gel databases

SWISS-2DPAGE

P0A6E6.

Genome annotation databases

GeneID

948245.

GenomeReviews

Gene locus JW3709 in contig AP009048_GR.
Gene locus b3731 in contig U00096_GR.

KEGG

ecj:JW3709.
eco:b3731.

Organism-specific databases

EchoBASE

EB0098.

EcoGene

EG10100. atpC.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6E6.

OMA

IHVDVVS.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPC-MON.

Gene expression databases

Genevestigator

P0A6E6.

Family and domain databases

HAMAP

MF_00530.
[Tree]

InterPro

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

Gene3D

G3DSA:1.20.5.440. ATPase_F1_d/e. 1 hit.
G3DSA:2.60.15.10. ATPase_F1_d/e. 1 hit.

PANTHER

PTHR13822. ATPase_F1_d/e. 1 hit.

Pfam

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

ProDom

PD000944. ATPsynt_DE. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01216. ATP_synt_epsi. 1 hit.

ProtoNet

Search...

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:	November 3, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)