ID   ATPD_ECOLI              Reviewed;         177 AA.
AC   P0ABA4; P00831; Q2M853;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE   AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE   AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE            Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN   Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; Synonyms=papE, uncH;
GN   OrderedLocusNames=b3735, JW3713;
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=6458296; DOI=10.1016/0006-291x(81)91504-7;
RA   Mabuchi K., Kanazawa H., Kayano T., Futai M.;
RT   "Nucleotide sequence of the gene coding for the delta subunit of proton
RT   translocating ATPase of Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 102:172-179(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 [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   [7]
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   [8]
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   [9]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BL21-DE3;
RX   PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA   Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA   von Heijne G., Daley D.O.;
RT   "Protein complexes of the Escherichia coli cell envelope.";
RL   J. Biol. Chem. 280:34409-34419(2005).
RN   [10]
RP   STRUCTURE BY NMR OF 1-135.
RX   PubMed=9164460; DOI=10.1038/nsb0397-198;
RA   Wilkens S., Dunn S.D., Chandler J., Dahlquist F.W., Capaldi R.A.;
RT   "Solution structure of the N-terminal domain of the delta subunit of the E.
RT   coli ATPsynthase.";
RL   Nat. Struct. Biol. 4:198-201(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: This protein is part of the stalk that links CF(0) to CF(1).
CC       It either transmits conformational changes from CF(0) to CF(1) or is
CC       implicated in proton conduction.
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(10-14). 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:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:16079137}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01416, ECO:0000269|PubMed:16079137}; Peripheral membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:16079137}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR   EMBL; J01594; AAA24734.1; -; Genomic_DNA.
DR   EMBL; M12212; AAA20044.1; -; Unassigned_DNA.
DR   EMBL; X01631; CAA25779.1; -; Genomic_DNA.
DR   EMBL; V00266; CAA23524.1; -; Genomic_DNA.
DR   EMBL; V00264; CAA23517.1; -; Genomic_DNA.
DR   EMBL; M25464; AAA83872.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62087.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76758.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77553.1; -; Genomic_DNA.
DR   PIR; A93732; PWECD.
DR   RefSeq; NP_418191.1; NC_000913.3.
DR   RefSeq; WP_001288587.1; NZ_STEB01000015.1.
DR   PDB; 1ABV; NMR; -; A=2-135.
DR   PDB; 2A7U; NMR; -; B=2-135.
DR   PDB; 5T4O; EM; 6.90 A; L=1-177.
DR   PDB; 5T4P; EM; 7.77 A; L=1-177.
DR   PDB; 5T4Q; EM; 8.53 A; L=1-177.
DR   PDB; 6OQR; EM; 3.10 A; W=1-177.
DR   PDB; 6OQS; EM; 3.30 A; W=1-177.
DR   PDB; 6OQT; EM; 3.10 A; W=1-177.
DR   PDB; 6OQU; EM; 3.20 A; W=1-177.
DR   PDB; 6OQV; EM; 3.30 A; W=1-177.
DR   PDB; 6OQW; EM; 3.10 A; W=1-177.
DR   PDB; 6PQV; EM; 3.30 A; W=1-177.
DR   PDB; 6WNQ; EM; 3.40 A; W=1-177.
DR   PDB; 6WNR; EM; 3.30 A; W=1-177.
DR   PDB; 8DBS; EM; 3.50 A; W=3-175.
DR   PDBsum; 1ABV; -.
DR   PDBsum; 2A7U; -.
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; 6WNQ; -.
DR   PDBsum; 6WNR; -.
DR   PDBsum; 8DBS; -.
DR   AlphaFoldDB; P0ABA4; -.
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-21854; -.
DR   EMDB; EMD-21855; -.
DR   EMDB; EMD-8357; -.
DR   EMDB; EMD-8358; -.
DR   EMDB; EMD-8359; -.
DR   SMR; P0ABA4; -.
DR   BioGRID; 4262111; 51.
DR   BioGRID; 852556; 6.
DR   ComplexPortal; CPX-4022; ATP synthase complex.
DR   DIP; DIP-47921N; -.
DR   IntAct; P0ABA4; 13.
DR   STRING; 511145.b3735; -.
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; P0ABA4; -.
DR   PaxDb; 511145-b3735; -.
DR   EnsemblBacteria; AAC76758; AAC76758; b3735.
DR   GeneID; 83578725; -.
DR   GeneID; 948254; -.
DR   KEGG; ecj:JW3713; -.
DR   KEGG; eco:b3735; -.
DR   PATRIC; fig|1411691.4.peg.2965; -.
DR   EchoBASE; EB0103; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_3_0_6; -.
DR   InParanoid; P0ABA4; -.
DR   OMA; MVDNIQD; -.
DR   OrthoDB; 9816221at2; -.
DR   PhylomeDB; P0ABA4; -.
DR   BioCyc; EcoCyc:ATPH-MONOMER; -.
DR   BioCyc; MetaCyc:ATPH-MONOMER; -.
DR   EvolutionaryTrace; P0ABA4; -.
DR   PRO; PR:P0ABA4; -.
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:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IMP:EcoliWiki.
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; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR   PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR   PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..177
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000193462"
FT   CONFLICT        82
FT                   /note="E -> D (in Ref. 4; AAA20044)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..21
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           25..39
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           42..47
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           54..62
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           72..83
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           89..103
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          149..155
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           164..174
FT                   /evidence="ECO:0007829|PDB:6OQR"
SQ   SEQUENCE   177 AA;  19332 MW;  6AFD9552A79C81A5 CRC64;
     MSEFITVARP YAKAAFDFAV EHQSVERWQD MLAFAAEVTK NEQMAELLSG ALAPETLAES
     FIAVCGEQLD ENGQNLIRVM AENGRLNALP DVLEQFIHLR AVSEATAEVD VISAAALSEQ
     QLAKISAAME KRLSRKVKLN CKIDKSVMAG VIIRAGDMVI DGSVRGRLER LADVLQS
//