P68699 (ATPL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit c

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

Gene names

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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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-Rule 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-Rule 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 c10. 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 reversibly protonated aspartate residue inhibits ATPase in vitro. HAMAP-Rule MF_01396 In this organism c-rings of between c8 and c12 can be isolated in vivo following experimental manipulations, however only c8 and c9, in addition to c10, are partially functional (Ref.12). HAMAP-Rule 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 Transmembrane helix
Ligand	Lipid-binding
PTM	Formylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from direct assay PubMed 2863271. Source: EcoliWiki plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from mutant phenotype PubMed 6460031. Source: EcoliWiki
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase activity, rotational mechanism Inferred from mutant phenotype PubMed 2863271. Source: EcoCyc proton-transporting ATPase activity, rotational mechanism Inferred from mutant phenotype PubMed 6460031. Source: EcoCyc
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-Rule MF_01396

PRO_0000112144

Regions

Topological domain

1 – 10

10

Periplasmic HAMAP-Rule MF_01396

Transmembrane

11 – 31

21

Helical HAMAP-Rule MF_01396

Topological domain

32 – 52

21

Cytoplasmic HAMAP-Rule MF_01396

Transmembrane

53 – 73

21

Helical HAMAP-Rule MF_01396

Topological domain

74 – 79

6

Periplasmic HAMAP-Rule MF_01396

Sites

Site

61

1

Reversibly protonated during proton transport

Amino acid modifications

Modified residue

1

1

N-formylmethionine HAMAP-Rule 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

76

1

F → S in CAA23591. 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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

NP_418193.1. NC_000913.2.
YP_491692.1. NC_007779.1.

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	[»]

ProteinModelPortal

P68699.

SMR

P68699. Positions 1-79.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68699. 2 interactions.

MINT

MINT-8087956.

STRING

511145.b3737.

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.

Proteomic databases

PaxDb

P68699.

PRIDE

P68699.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76760; AAC76760; b3737.
BAE77551; BAE77551; BAE77551.

GeneID

12933605.
948253.

KEGG

ecj:Y75_p3431.
eco:b3737.

PATRIC

32122971. VBIEscCol129921_3861.

Organism-specific databases

EchoBASE

EB0100.

EcoGene

EG10102. atpE.

Phylogenomic databases

eggNOG

COG0636.

HOGENOM

HOG000235244.

KO

K02110.

OMA

VDAVPMI.

ProtClustDB

PRK06876.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPE-MONOMER.
ECOL316407:JW3715-MONOMER.
MetaCyc:ATPE-MONOMER.

Gene expression databases

Genevestigator

P68699.

Family and domain databases

Gene3D

1.20.20.10. 1 hit.

HAMAP

MF_01396. ATP_synth_c_bact.

InterPro

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

Pfam

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

PRINTS

PR00124. ATPASEC.

SUPFAM

SSF81333. ATPase_F0/V0_c. 1 hit.

TIGRFAMs

TIGR01260. ATP_synt_c. 1 hit.

PROSITE

PS00605. ATPASE_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P68699.

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:	May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program