Reviewed, UniProtKB/Swiss-Prot P68699 (ATPL_ECOLI)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit c
Alternative name(s):
    ATP synthase F(0) sector subunit c
    F-type ATPase subunit c
      Short name=F-ATPase subunit c
    Lipid-binding protein
    Dicyclohexylcarbodiimide-binding protein

Gene names

Name:	atpE
Synonyms:	papH, uncE
Ordered Locus Names:	b3737, JW3715

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	79 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 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 c(10). 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 active aspartate residue inhibits ATPase in vitro. HAMAP MF_01396 In this organism c-rings of between c8 and c(12) can be isolated in vivo following experimental manipulations, however only c8 and c9, in additon to c(10), are partially functional (Ref.12). HAMAP MF_01396
Sequence similarities	Belongs to the ATPase C chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Ligand	Lipid-binding
PTM	Formylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from mutant phenotype. Source: UniProtKB
Cellular component	integral to membrane Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, coupling factor F(o) Inferred from mutant phenotype. Source: UniProtKB
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 79

79

ATP synthase subunit c HAMAP MF_01396

PRO_0000112144

Regions

Topological domain

1 – 10

10

Periplasmic HAMAP MF_01396

Transmembrane

11 – 31

21

HAMAP MF_01396

Topological domain

32 – 52

21

Cytoplasmic HAMAP MF_01396

Transmembrane

53 – 73

21

HAMAP MF_01396

Topological domain

74 – 79

6

Periplasmic HAMAP MF_01396

Sites

Site

61

1

Reversibly protonated during proton transport HAMAP MF_01396

Amino acid modifications

Modified residue

1

1

N-formylmethionine HAMAP MF_01396

Experimental info

Mutagenesis

23

1

G → D in uncE429; unable to assemble in the membrane. Ref.8

Mutagenesis

28

1

I → V in DC1; has a functional F0 as well as F1 part. However, the ATPase activity is inhibited. Ref.7

Mutagenesis

31

1

L → F in uncE408 and uncE463; unable to assemble in the membrane. Ref.8

Mutagenesis

61

1

D → G in DG 7/1; contains an enzymatically active F1 component, but no functional F0 component. Ref.7

Sequence conflict

37

1

E → Q Ref.2

Secondary structure

1

.

.

.

.

.

.

79

Helix Strand Turn

Details...

Helix

2 – 39

38

Beta strand

44 – 46

3

Helix

47 – 78

32

Sequences

	Sequence		Length	Mass (Da)
	P68699-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0F595A69D8AD1F9E	FASTA	79	8,256
	10 20 30 40 50 60 MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV 70 DAIPMIAVGL GLYVMFAVA

References

	« Hide 'large scale' referencesShow '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: 6266400] [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: 6278247] [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: 6272190] [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: 6193778] [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: 6395859] [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: 6446460] [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: 6309138] [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: 7686882] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 11320246] [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: 15919996] [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: 1385726] [Abstract] Cited for: STRUCTURE BY NMR, ACTIVE 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: 7849023] [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: 9636021] [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: 10580496] [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: 9237612] [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.

PIR

LWECA. B93732.

RefSeq

AP_004050.1.
NP_418193.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A91	NMR	-	A	1-79	[»]
1ATY	NMR	-	A	1-79	[»]
1C0V	NMR	-	A	1-79	[»]
1C17	NMR	-	A/B/C/D/E/F/G/H/I/J/K/L	1-79	[»]
1C99	NMR	-	A	1-79	[»]
1IJP	NMR	-	A	1-79	[»]
1J7F	model	-	A/B/C/D/E/F/G/H/I/J/K/L	1-79	[»]
1L6T	NMR	-	A	1-79	[»]
1QO1	X-ray	3.90	K/L/M/N/O/P/Q/R/S/T	1-79	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P68699.

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.

Genome annotation databases

GeneID

948253.

GenomeReviews

Gene locus JW3715 in contig AP009048_GR.
Gene locus b3737 in contig U00096_GR.

KEGG

ecj:JW3715.
eco:b3737.

Organism-specific databases

EchoBASE

EB0100.

EcoGene

EG10102. atpE.

CMR

Search...

Phylogenomic databases

eggNOG

COG0636.

HOGENOM

HBG753983.

OMA

FFIMMGL.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPE-MONOMER.
ECOL168927:B3737-MONOMER.
MetaCyc:ATPE-MONOMER.

Gene expression databases

Genevestigator

P68699.

Family and domain databases

HAMAP

MF_01396. ATP_synth_c_bact.
[Tree]

InterPro

IPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_F0/V0-cplx_csu.
[Graphical view]

Gene3D

G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.

Pfam

PF00137. ATP-synt_C. 1 hit.
[Graphical view]

PRINTS

PR00124. ATPASEC.

TIGRFAMs

TIGR01260. ATP_synt_c. 1 hit.

PROSITE

PS00605. ATPASE_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ATPL_ECOLI

Accession

Primary (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:	February 9, 2010
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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