GENTAUR Molecular Products.

 ATPL_ECOLI              Reviewed;          79 AA.
 P68699; P00844; Q2M855;
 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
 21-JUL-1986, sequence version 1.
 25-APR-2018, entry version 119.
 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.
 Gene3D; 1.20.20.10; -; 1.
 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; IPR038662; ATP_synth_F0_csu_sf.
 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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