ID   ATP6_ECOLI              Reviewed;         271 AA.
AC   P0AB98; P00855; Q2M856; Q47065; Q47708;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; Synonyms=papD, uncB;
GN   OrderedLocusNames=b3738, JW3716;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
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   [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=6277311; DOI=10.1016/0006-291x(81)90495-2;
RA   Kanazawa H., Mabuchi K., Kayano T., Noumi T., Sekiya T., Futai M.;
RT   "Nucleotide sequence of the genes for F0 components of the proton-
RT   translocating ATPase from Escherichia coli: prediction of the primary
RT   structure of F0 subunits.";
RL   Biochem. Biophys. Res. Commun. 103:613-620(1981).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6301339; DOI=10.1111/j.1749-6632.1982.tb25731.x;
RA   Kanazawa H., Futai M.;
RT   "Structure and function of H+-ATPase: what we have learned from Escherichia
RT   coli H+-ATPase.";
RL   Ann. N. Y. Acad. Sci. 402:45-64(1982).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RX   PubMed=2874137; DOI=10.1016/s0021-9258(18)67488-5;
RA   Cai B.D., Simoni R.D.;
RT   "Impaired proton conductivity resulting from mutations in the a subunit of
RT   F1F0 ATPase in Escherichia coli.";
RL   J. Biol. Chem. 261:10043-10050(1986).
RN   [7]
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   [8]
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   [9]
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   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
RX   PubMed=6325392; DOI=10.1128/jb.158.1.300-306.1984;
RA   Kanazawa H., Kiyasu T., Noumi T., Futai M.;
RT   "Overproduction of subunit a of the F0 component of proton-translocating
RT   ATPase inhibits growth of Escherichia coli cells.";
RL   J. Bacteriol. 158:300-306(1984).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC   STRAIN=K12;
RX   PubMed=6318052; DOI=10.1007/bf00327415;
RA   Nielsen J., Joergensen B.B., von Meyenburg K., Hansen F.G.;
RT   "The promoters of the atp operon of Escherichia coli K12.";
RL   Mol. Gen. Genet. 193:64-71(1984).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-271.
RX   PubMed=2874136; DOI=10.1016/s0021-9258(18)67487-3;
RA   Kumamoto C.A., Simoni R.D.;
RT   "Genetic evidence for interaction between the a and b subunits of the F0
RT   portion of the Escherichia coli proton translocating ATPase.";
RL   J. Biol. Chem. 261:10037-10042(1986).
RN   [13]
RP   MUTAGENESIS.
RX   PubMed=2536742; DOI=10.1016/s0021-9258(18)94065-2;
RA   Cain B.D., Simoni R.D.;
RT   "Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic
RT   analysis of the a subunit.";
RL   J. Biol. Chem. 264:3292-3300(1989).
RN   [14]
RP   MUTAGENESIS.
RX   PubMed=1829729; DOI=10.1128/jb.173.14.4544-4548.1991;
RA   Vik S.B., Lee D., Marshall P.A.;
RT   "Temperature-sensitive mutations at the carboxy terminus of the alpha
RT   subunit of the Escherichia coli F1F0 ATP synthase.";
RL   J. Bacteriol. 173:4544-4548(1991).
RN   [15]
RP   TOPOLOGY.
RX   PubMed=2162353; DOI=10.1016/s0021-9258(18)86981-2;
RA   Lewis M.L., Chang J.A., Simoni R.D.;
RT   "A topological analysis of subunit alpha from Escherichia coli F1F0-ATP
RT   synthase predicts eight transmembrane segments.";
RL   J. Biol. Chem. 265:10541-10550(1990).
RN   [16]
RP   TOPOLOGY.
RX   PubMed=2137094; DOI=10.1016/0014-5793(90)80058-q;
RA   Bjorbaek C., Foersom V., Michelsen O.;
RT   "The transmembrane topology of the a subunit from the ATPase in Escherichia
RT   coli analyzed by PhoA protein fusions.";
RL   FEBS Lett. 260:31-34(1990).
RN   [17]
RP   TOPOLOGY.
RX   PubMed=8706824; DOI=10.1016/0014-5793(96)00621-7;
RA   Yamada H., Moriyama Y., Maeda M., Futai M.;
RT   "Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase)
RT   subunit a.";
RL   FEBS Lett. 390:34-38(1996).
RN   [18]
RP   TOPOLOGY.
RX   PubMed=9632683; DOI=10.1074/jbc.273.26.16241;
RA   Valiyaveetil F.I., Fillingame R.H.;
RT   "Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP
RT   synthase.";
RL   J. Biol. Chem. 273:16241-16247(1998).
RN   [19]
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   [20]
RP   STRUCTURE BY NMR OF 95-271.
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).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01393, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_01393, ECO:0000269|PubMed:15919996}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
CC   -!- CAUTION: Was originally proposed to be encoded from either Met-1 or
CC       Val-71 (PID CAA23521); it is now thought to start of Met-1.
CC       {ECO:0000305|PubMed:6278247}.
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DR   EMBL; J01594; AAA24731.1; -; Genomic_DNA.
DR   EMBL; X01631; CAA25776.1; -; Genomic_DNA.
DR   EMBL; V00264; CAA23514.1; -; Genomic_DNA.
DR   EMBL; V00266; CAA23520.1; -; Genomic_DNA.
DR   EMBL; V00266; CAA23521.1; -; Genomic_DNA.
DR   EMBL; V00310; CAA23590.1; -; Genomic_DNA.
DR   EMBL; M25464; AAA83869.2; -; Genomic_DNA.
DR   EMBL; M14019; AAA24740.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62090.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76761.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77550.1; -; Genomic_DNA.
DR   EMBL; X01383; CAA25641.1; -; Genomic_DNA.
DR   EMBL; M29174; AAA24423.1; -; Genomic_DNA.
DR   PIR; C93732; LWEC6.
DR   RefSeq; NP_418194.1; NC_000913.3.
DR   RefSeq; WP_000135625.1; NZ_SSZK01000036.1.
DR   PDB; 1C17; NMR; -; M=95-271.
DR   PDB; 5T4O; EM; 6.90 A; K=1-271.
DR   PDB; 5T4P; EM; 7.77 A; K=1-271.
DR   PDB; 5T4Q; EM; 8.53 A; K=1-271.
DR   PDB; 6OQR; EM; 3.10 A; a=1-271.
DR   PDB; 6OQS; EM; 3.30 A; a=1-271.
DR   PDB; 6OQT; EM; 3.10 A; a=1-271.
DR   PDB; 6OQU; EM; 3.20 A; a=1-271.
DR   PDB; 6OQV; EM; 3.30 A; a=1-271.
DR   PDB; 6OQW; EM; 3.10 A; a=1-271.
DR   PDB; 6PQV; EM; 3.30 A; a=1-271.
DR   PDB; 6VWK; EM; 3.30 A; a=1-271.
DR   PDB; 6WNQ; EM; 3.40 A; a=1-271.
DR   PDB; 6WNR; EM; 3.30 A; a=1-271.
DR   PDBsum; 1C17; -.
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; P0AB98; -.
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; P0AB98; -.
DR   BioGRID; 4262600; 50.
DR   ComplexPortal; CPX-4022; ATP synthase complex.
DR   DIP; DIP-47956N; -.
DR   IntAct; P0AB98; 2.
DR   MINT; P0AB98; -.
DR   STRING; 511145.b3738; -.
DR   ChEMBL; CHEMBL1075074; -.
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; P0AB98; -.
DR   PaxDb; 511145-b3738; -.
DR   EnsemblBacteria; AAC76761; AAC76761; b3738.
DR   GeneID; 75205456; -.
DR   GeneID; 948252; -.
DR   KEGG; ecj:JW3716; -.
DR   KEGG; eco:b3738; -.
DR   PATRIC; fig|1411691.4.peg.2962; -.
DR   EchoBASE; EB0097; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_1_0_6; -.
DR   InParanoid; P0AB98; -.
DR   OMA; GFFWAAF; -.
DR   OrthoDB; 9789241at2; -.
DR   PhylomeDB; P0AB98; -.
DR   BioCyc; EcoCyc:ATPB-MONOMER; -.
DR   BioCyc; MetaCyc:ATPB-MONOMER; -.
DR   EvolutionaryTrace; P0AB98; -.
DR   PRO; PR:P0AB98; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:EcoCyc.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:EcoCyc.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IMP:EcoCyc.
DR   CDD; cd00310; ATP-synt_Fo_a_6; 1.
DR   Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   NCBIfam; TIGR01131; ATP_synt_6_or_A; 1.
DR   PANTHER; PTHR42823; ATP SYNTHASE SUBUNIT A, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42823:SF3; ATP SYNTHASE SUBUNIT A, CHLOROPLASTIC; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..271
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082053"
FT   TOPO_DOM        1..39
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        61..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        121..145
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        167..219
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        241
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        263..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         206
FT                   /note="S->L: Reduced activity."
FT   MUTAGEN         207
FT                   /note="L->Y,F: No change in activity."
FT   MUTAGEN         210
FT                   /note="R->K,I,V,E: Completely defective."
FT   MUTAGEN         214
FT                   /note="N->H: Completely defective."
FT   MUTAGEN         214
FT                   /note="N->V: Reduced activity."
FT   MUTAGEN         217
FT                   /note="A->H: Reduced activity."
FT   MUTAGEN         217
FT                   /note="A->R: Completely defective."
FT   MUTAGEN         245
FT                   /note="H->Y: Reduced activity."
FT   CONFLICT        71
FT                   /note="V -> M (in Ref. 2; CAA23521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179..182
FT                   /note="TLQP -> RCST (in Ref. 4; CAA23590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="F -> S (in Ref. 6; AAA24740)"
FT                   /evidence="ECO:0000305"
FT   HELIX           8..14
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:6OQU"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:6WNR"
FT   STRAND          40..43
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           47..64
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           74..93
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           101..117
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           125..132
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           147..180
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   TURN            181..184
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           189..228
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           231..234
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           235..268
FT                   /evidence="ECO:0007829|PDB:6OQR"
SQ   SEQUENCE   271 AA;  30303 MW;  4933EAF09401566D CRC64;
     MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV VLGLLFLVLF
     RSVAKKATSG VPGKFQTAIE LVIGFVNGSV KDMYHGKSKL IAPLALTIFV WVFLMNLMDL
     LPIDLLPYIA EHVLGLPALR VVPSADVNVT LSMALGVFIL ILFYSIKMKG IGGFTKELTL
     QPFNHWAFIP VNLILEGVSL LSKPVSLGLR LFGNMYAGEL IFILIAGLLP WWSQWILNVP
     WAIFHILIIT LQAFIFMVLT IVYLSMASEE H
//