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ATP synthase subunit c (ATP synthase F(0) sector subunit c) (Dicyclohexylcarbodiimide-binding protein) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein)

 ATPL_ECOLI              Reviewed;          79 AA.
P68699; P00844; Q2M855;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
28-MAR-2018, entry version 118.
RecName: Full=ATP synthase subunit c;
AltName: Full=ATP synthase F(0) sector subunit c;
AltName: Full=Dicyclohexylcarbodiimide-binding protein;
AltName: Full=F-type ATPase subunit c;
Short=F-ATPase subunit c;
AltName: Full=Lipid-binding protein;
Name=atpE; Synonyms=papH, uncE; OrderedLocusNames=b3737, JW3715;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
PROTEIN SEQUENCE.
Sebald W., Hoppe J., Wachter E.;
"Amino acid sequence of the ATPase proteolipid from mitochondria,
chloroplasts and bacteria (wild type and mutants).";
(In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.);
Function and molecular aspects of biomembrane transport, pp.63-74,
Elsevier, Amsterdam (1979).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6266400; DOI=10.1016/S0006-291X(81)80085-X;
Kanazawa H., Mabuchi K., Kayano T., Tamura F., Futai M.;
"Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-
binding protein and the alpha subunit of proton-translocating ATPase
of Escherichia coli.";
Biochem. Biophys. Res. Commun. 100:219-225(1981).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6278247; DOI=10.1007/BF00271191;
Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.;
"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.";
Mol. Gen. Genet. 184:33-39(1981).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6272190; DOI=10.1093/nar/9.16.3919;
Gay N.J., Walker J.E.;
"The atp operon: nucleotide sequence of the promoter and the genes for
the membrane proteins, and the delta subunit of Escherichia coli ATP-
synthase.";
Nucleic Acids Res. 9:3919-3926(1981).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6193778; DOI=10.1042/bj2130451;
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.;
"The F1F0-ATPase of Escherichia coli. Substitution of proline by
leucine at position 64 in the c-subunit causes loss of oxidative
phosphorylation.";
Biochem. J. 213:451-458(1983).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6395859; DOI=10.1042/bj2240799;
Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
"DNA sequence around the Escherichia coli unc operon. Completion of
the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS
and phoS.";
Biochem. J. 224:799-815(1984).
[7]
PROTEIN SEQUENCE, AND MUTAGENESIS OF ILE-28 AND ASP-61.
STRAIN=K12;
PubMed=6446460; DOI=10.1016/0014-5793(80)80606-5;
Wachter E., Schmid R., Deckers G., Altendorf K.;
"Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins
from mutant strains of Escherichia coli defective in the energy-
transducing ATPase complex.";
FEBS Lett. 113:265-270(1980).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-23 AND
LEU-31.
PubMed=6309138; DOI=10.1042/bj2110717;
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.;
"Mutations in the uncE gene affecting assembly of the c-subunit of the
adenosine triphosphatase of Escherichia coli.";
Biochem. J. 211:717-726(1983).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7686882; DOI=10.1006/geno.1993.1230;
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
"DNA sequence and analysis of 136 kilobases of the Escherichia coli
genome: organizational symmetry around the origin of replication.";
Genomics 16:551-561(1993).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[12]
SUBUNIT, AND SUBUNIT C FUSIONS.
PubMed=11320246; DOI=10.1073/pnas.081424898;
Jiang W., Hermolin J., Fillingame R.H.;
"The preferred stoichiometry of c subunits in the rotary motor sector
of Escherichia coli ATP synthase is 10.";
Proc. Natl. Acad. Sci. U.S.A. 98:4966-4971(2001).
[13]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[14]
STRUCTURE BY NMR, AND SITE.
PubMed=1385726; DOI=10.1021/bi00142a017;
Norwood T.J., Crawford D.A., Steventon M.E., Driscoll P.C.,
Campbell I.D.;
"Heteronuclear 1H-15N nuclear magnetic resonance studies of the c
subunit of the Escherichia coli F1F0 ATP synthase: assignment and
secondary structure.";
Biochemistry 31:6285-6290(1992).
[15]
STRUCTURE BY NMR.
PubMed=7849023; DOI=10.1021/bi00005a020;
Girvin M.E., Fillingame R.H.;
"Determination of local protein structure by spin label difference 2D
NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP
synthase.";
Biochemistry 34:1635-1645(1995).
[16]
STRUCTURE BY NMR.
PubMed=9636021; DOI=10.1021/bi980511m;
Girvin M.E., Rastogi V.K., Abildgaard F., Markley J.L.,
Fillingame R.H.;
"Solution structure of the transmembrane H+-transporting subunit c of
the F1F0 ATP synthase.";
Biochemistry 37:8817-8824(1998).
[17]
STRUCTURE BY NMR.
PubMed=10580496; DOI=10.1038/46224;
Rastogi V.K., Girvin M.E.;
"Structural changes linked to proton translocation by subunit c of the
ATP synthase.";
Nature 402:263-268(1999).
[18]
3D-STRUCTURE MODELING.
PubMed=9237612; DOI=10.1016/S0014-5793(97)00529-2;
Groth G., Walker J.E.;
"Model of the c-subunit oligomer in the membrane domain of F-
ATPases.";
FEBS Lett. 410:117-123(1997).
-!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
presence of a proton or sodium gradient. F-type ATPases consist of
two structural domains, F(1) containing the extramembraneous
catalytic core and F(0) containing the membrane proton channel,
linked together by a central stalk and a peripheral stalk. During
catalysis, ATP synthesis in the catalytic domain of F(1) is
coupled via a rotary mechanism of the central stalk subunits to
proton translocation.
-!- FUNCTION: Key component of the F(0) 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 F(1)
delta and epsilon subunits.
-!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
core - and F(0) - the membrane proton channel. F(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
has three main subunits: a(1), b(2) and c(10). The alpha and beta
chains form an alternating ring which encloses part of the gamma
chain. F(1) is attached to F(0) by a central stalk formed by the
gamma and epsilon chains, while a peripheral stalk is formed by
the delta and b chains. {ECO:0000269|PubMed:11320246}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
{ECO:0000269|PubMed:15919996}.
-!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) binding to the
reversibly protonated aspartate residue inhibits ATPase in vitro.
-!- MISCELLANEOUS: In this organism c-rings of between c(8) and c(12)
can be isolated in vivo following experimental manipulations,
however only c(8) and c(9), in addition to c(10), are partially
functional. {ECO:0000305|PubMed:11320246}.
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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EMBL; J01594; AAA24732.1; -; Genomic_DNA.
EMBL; V00310; CAA23591.1; -; Genomic_DNA.
EMBL; M25464; AAA83870.1; -; Genomic_DNA.
EMBL; M12214; AAA23668.1; -; Genomic_DNA.
EMBL; V00266; CAA23522.1; -; Genomic_DNA.
EMBL; V00264; CAA23515.1; -; Genomic_DNA.
EMBL; V01506; CAA24752.1; -; Genomic_DNA.
EMBL; X01631; CAA25777.1; -; Genomic_DNA.
EMBL; L10328; AAA62089.1; -; Genomic_DNA.
EMBL; U00096; AAC76760.1; -; Genomic_DNA.
EMBL; AP009048; BAE77551.1; -; Genomic_DNA.
PIR; B93732; LWECA.
RefSeq; NP_418193.1; NC_000913.3.
RefSeq; WP_000429386.1; NZ_LN832404.1.
PDB; 1A91; NMR; -; A=1-79.
PDB; 1ATY; NMR; -; A=1-79.
PDB; 1C0V; NMR; -; A=1-79.
PDB; 1C17; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L=1-79.
PDB; 1C99; NMR; -; A=1-79.
PDB; 1IJP; NMR; -; A=1-79.
PDB; 1J7F; Model; -; A/B/C/D/E/F/G/H/I/J/K/L=1-79.
PDB; 1L6T; NMR; -; A=1-79.
PDB; 1QO1; X-ray; 3.90 A; K/L/M/N/O/P/Q/R/S/T=1-79.
PDB; 4UTQ; EM; 8.00 A; Z=1-79.
PDB; 5T4O; EM; 6.90 A; M/N/O/P/Q/R/S/T/U/V=1-79.
PDB; 5T4P; EM; 7.77 A; M/N/O/P/Q/R/S/T/U/V=1-79.
PDB; 5T4Q; EM; 8.53 A; M/N/O/P/Q/R/S/T/U/V=1-79.
PDBsum; 1A91; -.
PDBsum; 1ATY; -.
PDBsum; 1C0V; -.
PDBsum; 1C17; -.
PDBsum; 1C99; -.
PDBsum; 1IJP; -.
PDBsum; 1J7F; -.
PDBsum; 1L6T; -.
PDBsum; 1QO1; -.
PDBsum; 4UTQ; -.
PDBsum; 5T4O; -.
PDBsum; 5T4P; -.
PDBsum; 5T4Q; -.
ProteinModelPortal; P68699; -.
SMR; P68699; -.
BioGrid; 4262599; 52.
DIP; DIP-2198N; -.
IntAct; P68699; 3.
MINT; P68699; -.
STRING; 316385.ECDH10B_3924; -.
TCDB; 3.A.2.1.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
PaxDb; P68699; -.
PRIDE; P68699; -.
EnsemblBacteria; AAC76760; AAC76760; b3737.
EnsemblBacteria; BAE77551; BAE77551; BAE77551.
GeneID; 34151810; -.
GeneID; 948253; -.
KEGG; ecj:JW3715; -.
KEGG; eco:b3737; -.
PATRIC; fig|1411691.4.peg.2963; -.
EchoBASE; EB0100; -.
EcoGene; EG10102; atpE.
eggNOG; COG0636; LUCA.
HOGENOM; HOG000235244; -.
InParanoid; P68699; -.
KO; K02110; -.
OMA; NIATVGY; -.
BioCyc; EcoCyc:ATPE-MONOMER; -.
BioCyc; MetaCyc:ATPE-MONOMER; -.
EvolutionaryTrace; P68699; -.
PRO; PR:P68699; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IMP:EcoliWiki.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:EcoCyc.
GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:EcoCyc.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F/V-ATP_Csub_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
TIGRFAMs; TIGR01260; ATP_synt_c; 1.
PROSITE; PS00605; ATPASE_C; 1.
1: Evidence at protein level;
3D-structure; ATP synthesis; Cell inner membrane; Cell membrane;
CF(0); Complete proteome; Direct protein sequencing; Formylation;
Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 79 ATP synthase subunit c.
/FTId=PRO_0000112144.
TOPO_DOM 1 10 Periplasmic.
TRANSMEM 11 31 Helical.
TOPO_DOM 32 52 Cytoplasmic.
TRANSMEM 53 73 Helical.
TOPO_DOM 74 79 Periplasmic.
SITE 61 61 Reversibly protonated during proton
transport.
MOD_RES 1 1 N-formylmethionine. {ECO:0000250}.
MUTAGEN 23 23 G->D: In uncE429; unable to assemble in
the membrane.
{ECO:0000269|PubMed:6309138}.
MUTAGEN 28 28 I->V: In DC1; has a functional F0 as well
as F1 part. However, the ATPase activity
is inhibited.
{ECO:0000269|PubMed:6446460}.
MUTAGEN 31 31 L->F: In uncE408 and uncE463; unable to
assemble in the membrane.
{ECO:0000269|PubMed:6309138}.
MUTAGEN 61 61 D->G: In DG 7/1; contains an
enzymatically active F1 component, but no
functional F0 component.
{ECO:0000269|PubMed:6446460}.
CONFLICT 76 76 F -> S (in Ref. 2; CAA23591).
{ECO:0000305}.
HELIX 2 39 {ECO:0000244|PDB:1A91}.
STRAND 44 46 {ECO:0000244|PDB:1A91}.
HELIX 47 78 {ECO:0000244|PDB:1A91}.
SEQUENCE 79 AA; 8256 MW; 0F595A69D8AD1F9E CRC64;
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV
DAIPMIAVGL GLYVMFAVA


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