ATPD_DICDI
ID ATPD_DICDI Reviewed; 170 AA.
AC Q55F42;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP synthase subunit delta, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit delta {ECO:0000250|UniProtKB:P30049};
DE AltName: Full=F-ATPase delta subunit;
DE Flags: Precursor;
GN Name=atp5f1d {ECO:0000250|UniProtKB:P30049}; Synonyms=atp16, atp5D;
GN ORFNames=DDB_G0269038;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP turnover in
CC the catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(1) domain and of the central stalk which is part of the complex
CC rotary element. Rotation of the central stalk against the surrounding
CC alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC catalytic sites on the beta subunits (By similarity). {ECO:0000250}.
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, b and c (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR EMBL; AAFI02000004; EAL73108.1; -; Genomic_DNA.
DR RefSeq; XP_646828.1; XM_641736.1.
DR AlphaFoldDB; Q55F42; -.
DR SMR; Q55F42; -.
DR STRING; 44689.DDB0238330; -.
DR PaxDb; Q55F42; -.
DR EnsemblProtists; EAL73108; EAL73108; DDB_G0269038.
DR GeneID; 8616511; -.
DR KEGG; ddi:DDB_G0269038; -.
DR dictyBase; DDB_G0269038; atp5D.
DR eggNOG; KOG1758; Eukaryota.
DR HOGENOM; CLU_084338_0_0_1; -.
DR InParanoid; Q55F42; -.
DR OMA; TLPHQTI; -.
DR PhylomeDB; Q55F42; -.
DR PRO; PR:Q55F42; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; ISS:dictyBase.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISS:dictyBase.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; ISS:dictyBase.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 2.60.15.10; -; 1.
DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR PANTHER; PTHR13822; PTHR13822; 1.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF51344; SSF51344; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..170
FT /note="ATP synthase subunit delta, mitochondrial"
FT /id="PRO_0000328055"
SQ SEQUENCE 170 AA; 18508 MW; F97FFACEE466410A CRC64;
MIRSIIKSSN NLLKSNVAIN SNKRFFATEA SATSDLLTFS LLSPHQTIYK DKKAQLVTLP
GAKGIFGVAK NHVPRIAELK PGVIQINHEN GDLEKFFISG GFAFVNPDAS CYINTIEAVP
IDQLDAEEVK NGLARYTQLY NDAQEENAKA VALIGLETYQ QMAFACGVSA
