ATPL_ECOLI
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 03-AUG-2022, entry version 143.
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; Proteobacteria; 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}.
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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 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; P68699; -.
DR PRIDE; P68699; -.
DR EnsemblBacteria; AAC76760; AAC76760; b3737.
DR EnsemblBacteria; BAE77551; BAE77551; BAE77551.
DR GeneID; 64726533; -.
DR GeneID; 67517226; -.
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 PhylomeDB; P68699; -.
DR BioCyc; EcoCyc:ATPE-MON; -.
DR BioCyc; MetaCyc:ATPE-MON; -.
DR EvolutionaryTrace; P68699; -.
DR PRO; PR:P68699; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC: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 Gene3D; 1.20.20.10; -; 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 Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01260; ATP_synt_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
