ID   ATPL_ECOLI              Reviewed;          79 AA.
AC   P68699; P00844; Q2M855;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=ATP synthase subunit c;
DE   AltName: Full=ATP synthase F(0) sector subunit c;
DE   AltName: Full=Dicyclohexylcarbodiimide-binding protein;
DE   AltName: Full=F-type ATPase subunit c;
DE            Short=F-ATPase subunit c;
DE   AltName: Full=Lipid-binding protein;
GN   Name=atpE; Synonyms=papH, uncE; OrderedLocusNames=b3737, JW3715;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Sebald W., Hoppe J., Wachter E.;
RT   "Amino acid sequence of the ATPase proteolipid from mitochondria,
RT   chloroplasts and bacteria (wild type and mutants).";
RL   (In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.);
RL   Function and molecular aspects of biomembrane transport, pp.63-74,
RL   Elsevier, Amsterdam (1979).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6266400; DOI=10.1016/s0006-291x(81)80085-x;
RA   Kanazawa H., Mabuchi K., Kayano T., Tamura F., Futai M.;
RT   "Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-binding
RT   protein and the alpha subunit of proton-translocating ATPase of Escherichia
RT   coli.";
RL   Biochem. Biophys. Res. Commun. 100:219-225(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6278247; DOI=10.1007/bf00271191;
RA   Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.;
RT   "The nucleotide sequence of the atp genes coding for the F0 subunits a, b,
RT   c and the F1 subunit delta of the membrane bound ATP synthase of
RT   Escherichia coli.";
RL   Mol. Gen. Genet. 184:33-39(1981).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6272190; DOI=10.1093/nar/9.16.3919;
RA   Gay N.J., Walker J.E.;
RT   "The atp operon: nucleotide sequence of the promoter and the genes for the
RT   membrane proteins, and the delta subunit of Escherichia coli ATP-
RT   synthase.";
RL   Nucleic Acids Res. 9:3919-3926(1981).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6193778; DOI=10.1042/bj2130451;
RA   Fimmel A.L., Jans D.A., Langman L., James L.B., Ash G.R., Downie J.A.,
RA   Senior A.E., Gibson F., Cox G.B.;
RT   "The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at
RT   position 64 in the c-subunit causes loss of oxidative phosphorylation.";
RL   Biochem. J. 213:451-458(1983).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6395859; DOI=10.1042/bj2240799;
RA   Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT   "DNA sequence around the Escherichia coli unc operon. Completion of the
RT   sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT   phoS.";
RL   Biochem. J. 224:799-815(1984).
RN   [7]
RP   PROTEIN SEQUENCE, AND MUTAGENESIS OF ILE-28 AND ASP-61.
RC   STRAIN=K12;
RX   PubMed=6446460; DOI=10.1016/0014-5793(80)80606-5;
RA   Wachter E., Schmid R., Deckers G., Altendorf K.;
RT   "Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from
RT   mutant strains of Escherichia coli defective in the energy-transducing
RT   ATPase complex.";
RL   FEBS Lett. 113:265-270(1980).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-23 AND LEU-31.
RX   PubMed=6309138; DOI=10.1042/bj2110717;
RA   Jans D.A., Fimmel A.L., Langman L., James L.B., Downie J.A., Senior A.E.,
RA   Ash G.R., Gibson F., Cox G.B.;
RT   "Mutations in the uncE gene affecting assembly of the c-subunit of the
RT   adenosine triphosphatase of Escherichia coli.";
RL   Biochem. J. 211:717-726(1983).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [12]
RP   SUBUNIT, AND SUBUNIT C FUSIONS.
RX   PubMed=11320246; DOI=10.1073/pnas.081424898;
RA   Jiang W., Hermolin J., Fillingame R.H.;
RT   "The preferred stoichiometry of c subunits in the rotary motor sector of
RT   Escherichia coli ATP synthase is 10.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4966-4971(2001).
RN   [13]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [14]
RP   STRUCTURE BY NMR, AND SITE.
RX   PubMed=1385726; DOI=10.1021/bi00142a017;
RA   Norwood T.J., Crawford D.A., Steventon M.E., Driscoll P.C., Campbell I.D.;
RT   "Heteronuclear 1H-15N nuclear magnetic resonance studies of the c subunit
RT   of the Escherichia coli F1F0 ATP synthase: assignment and secondary
RT   structure.";
RL   Biochemistry 31:6285-6290(1992).
RN   [15]
RP   STRUCTURE BY NMR.
RX   PubMed=7849023; DOI=10.1021/bi00005a020;
RA   Girvin M.E., Fillingame R.H.;
RT   "Determination of local protein structure by spin label difference 2D NMR:
RT   the region neighboring Asp61 of subunit c of the F1F0 ATP synthase.";
RL   Biochemistry 34:1635-1645(1995).
RN   [16]
RP   STRUCTURE BY NMR.
RX   PubMed=9636021; DOI=10.1021/bi980511m;
RA   Girvin M.E., Rastogi V.K., Abildgaard F., Markley J.L., Fillingame R.H.;
RT   "Solution structure of the transmembrane H+-transporting subunit c of the
RT   F1F0 ATP synthase.";
RL   Biochemistry 37:8817-8824(1998).
RN   [17]
RP   STRUCTURE BY NMR.
RX   PubMed=10580496; DOI=10.1038/46224;
RA   Rastogi V.K., Girvin M.E.;
RT   "Structural changes linked to proton translocation by subunit c of the ATP
RT   synthase.";
RL   Nature 402:263-268(1999).
RN   [18]
RP   3D-STRUCTURE MODELING.
RX   PubMed=9237612; DOI=10.1016/s0014-5793(97)00529-2;
RA   Groth G., Walker J.E.;
RT   "Model of the c-subunit oligomer in the membrane domain of F-ATPases.";
RL   FEBS Lett. 410:117-123(1997).
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation.
CC   -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC       translocation across the membrane. A homomeric c-ring of 10 subunits
CC       forms the central stalk rotor element with the F(1) delta and epsilon
CC       subunits.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000269|PubMed:11320246}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15919996}.
CC   -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) binding to the
CC       reversibly protonated aspartate residue inhibits ATPase in vitro.
CC   -!- MISCELLANEOUS: In this organism c-rings of between c(8) and c(12) can
CC       be isolated in vivo following experimental manipulations, however only
CC       c(8) and c(9), in addition to c(10), are partially functional.
CC       {ECO:0000305|PubMed:11320246}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J01594; AAA24732.1; -; Genomic_DNA.
DR   EMBL; V00310; CAA23591.1; -; Genomic_DNA.
DR   EMBL; M25464; AAA83870.1; -; Genomic_DNA.
DR   EMBL; M12214; AAA23668.1; -; Genomic_DNA.
DR   EMBL; V00266; CAA23522.1; -; Genomic_DNA.
DR   EMBL; V00264; CAA23515.1; -; Genomic_DNA.
DR   EMBL; V01506; CAA24752.1; -; Genomic_DNA.
DR   EMBL; X01631; CAA25777.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62089.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76760.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77551.1; -; Genomic_DNA.
DR   PIR; B93732; LWECA.
DR   RefSeq; NP_418193.1; NC_000913.3.
DR   RefSeq; WP_000429386.1; NZ_STEB01000015.1.
DR   PDB; 1A91; NMR; -; A=1-79.
DR   PDB; 1ATY; NMR; -; A=1-79.
DR   PDB; 1C0V; NMR; -; A=1-79.
DR   PDB; 1C17; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L=1-79.
DR   PDB; 1C99; NMR; -; A=1-79.
DR   PDB; 1IJP; NMR; -; A=1-79.
DR   PDB; 1L6T; NMR; -; A=1-79.
DR   PDB; 1QO1; X-ray; 3.90 A; K/L/M/N/O/P/Q/R/S/T=1-79.
DR   PDB; 4UTQ; EM; 8.00 A; Z=1-79.
DR   PDB; 5T4O; EM; 6.90 A; M/N/O/P/Q/R/S/T/U/V=1-79.
DR   PDB; 5T4P; EM; 7.77 A; M/N/O/P/Q/R/S/T/U/V=1-79.
DR   PDB; 5T4Q; EM; 8.53 A; M/N/O/P/Q/R/S/T/U/V=1-79.
DR   PDB; 6OQR; EM; 3.10 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6OQS; EM; 3.30 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6OQT; EM; 3.10 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6OQU; EM; 3.20 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6OQV; EM; 3.30 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6OQW; EM; 3.10 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6PQV; EM; 3.30 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6VWK; EM; 3.30 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6WNQ; EM; 3.40 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDB; 6WNR; EM; 3.30 A; I/J/L/M/N/O/P/Q/R/S=1-79.
DR   PDBsum; 1A91; -.
DR   PDBsum; 1ATY; -.
DR   PDBsum; 1C0V; -.
DR   PDBsum; 1C17; -.
DR   PDBsum; 1C99; -.
DR   PDBsum; 1IJP; -.
DR   PDBsum; 1L6T; -.
DR   PDBsum; 1QO1; -.
DR   PDBsum; 4UTQ; -.
DR   PDBsum; 5T4O; -.
DR   PDBsum; 5T4P; -.
DR   PDBsum; 5T4Q; -.
DR   PDBsum; 6OQR; -.
DR   PDBsum; 6OQS; -.
DR   PDBsum; 6OQT; -.
DR   PDBsum; 6OQU; -.
DR   PDBsum; 6OQV; -.
DR   PDBsum; 6OQW; -.
DR   PDBsum; 6PQV; -.
DR   PDBsum; 6VWK; -.
DR   PDBsum; 6WNQ; -.
DR   PDBsum; 6WNR; -.
DR   AlphaFoldDB; P68699; -.
DR   EMDB; EMD-20167; -.
DR   EMDB; EMD-20168; -.
DR   EMDB; EMD-20169; -.
DR   EMDB; EMD-20170; -.
DR   EMDB; EMD-20171; -.
DR   EMDB; EMD-20172; -.
DR   EMDB; EMD-20454; -.
DR   EMDB; EMD-21419; -.
DR   EMDB; EMD-21854; -.
DR   EMDB; EMD-21855; -.
DR   EMDB; EMD-8357; -.
DR   EMDB; EMD-8358; -.
DR   EMDB; EMD-8359; -.
DR   SMR; P68699; -.
DR   BioGRID; 4262599; 52.
DR   ComplexPortal; CPX-4022; ATP synthase complex.
DR   DIP; DIP-2198N; -.
DR   IntAct; P68699; 3.
DR   MINT; P68699; -.
DR   STRING; 511145.b3737; -.
DR   TCDB; 3.A.2.1.1; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   jPOST; P68699; -.
DR   PaxDb; 511145-b3737; -.
DR   EnsemblBacteria; AAC76760; AAC76760; b3737.
DR   GeneID; 85164562; -.
DR   GeneID; 948253; -.
DR   KEGG; ecj:JW3715; -.
DR   KEGG; eco:b3737; -.
DR   PATRIC; fig|1411691.4.peg.2963; -.
DR   EchoBASE; EB0100; -.
DR   eggNOG; ENOG5032S3K; Bacteria.
DR   HOGENOM; CLU_148047_1_0_6; -.
DR   InParanoid; P68699; -.
DR   OMA; VTDGAFI; -.
DR   OrthoDB; 9811659at2; -.
DR   PhylomeDB; P68699; -.
DR   BioCyc; EcoCyc:ATPE-MONOMER; -.
DR   BioCyc; MetaCyc:ATPE-MONOMER; -.
DR   EvolutionaryTrace; P68699; -.
DR   PRO; PR:P68699; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:ComplexPortal.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IMP:EcoliWiki.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:EcoCyc.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:EcoCyc.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IMP:ComplexPortal.
DR   CDD; cd18185; ATP-synt_Fo_c_ATPE; 1.
DR   Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   NCBIfam; TIGR01260; ATP_synt_c; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Direct protein sequencing; Formylation; Hydrogen ion transport;
KW   Ion transport; Lipid-binding; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..79
FT                   /note="ATP synthase subunit c"
FT                   /id="PRO_0000112144"
FT   TOPO_DOM        1..10
FT                   /note="Periplasmic"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT   TOPO_DOM        32..52
FT                   /note="Cytoplasmic"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT   TOPO_DOM        74..79
FT                   /note="Periplasmic"
FT   SITE            61
FT                   /note="Reversibly protonated during proton transport"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         23
FT                   /note="G->D: In uncE429; unable to assemble in the
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:6309138"
FT   MUTAGEN         28
FT                   /note="I->V: In DC1; has a functional F0 as well as F1
FT                   part. However, the ATPase activity is inhibited."
FT                   /evidence="ECO:0000269|PubMed:6446460"
FT   MUTAGEN         31
FT                   /note="L->F: In uncE408 and uncE463; unable to assemble in
FT                   the membrane."
FT                   /evidence="ECO:0000269|PubMed:6309138"
FT   MUTAGEN         61
FT                   /note="D->G: In DG 7/1; contains an enzymatically active F1
FT                   component, but no functional F0 component."
FT                   /evidence="ECO:0000269|PubMed:6446460"
FT   CONFLICT        76
FT                   /note="F -> S (in Ref. 2; CAA23591)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..41
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:6OQS"
FT   HELIX           46..60
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           62..75
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:6OQR"
SQ   SEQUENCE   79 AA;  8256 MW;  0F595A69D8AD1F9E CRC64;
     MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV
     DAIPMIAVGL GLYVMFAVA
//