ID   ATP4_ARATH              Reviewed;         203 AA.
AC   Q96252;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=ATP synthase subunit delta', mitochondrial;
DE   AltName: Full=F-ATPase delta' subunit;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g47030; ORFNames=MQD22.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Sakamoto W., Wintz H.;
RT   "Nucleotide sequence of cDNAs encoding gamma, delta, delta-prime, and
RT   epsilon subunits of mitochondrial F1-ATPase in Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR96-125(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 27-41, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf, and Stem;
RX   PubMed=11743114; DOI=10.1104/pp.010474;
RA   Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT   "Proteomic approach to identify novel mitochondrial proteins in
RT   Arabidopsis.";
RL   Plant Physiol. 127:1694-1710(2001).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
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.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; D88376; BAA13601.1; -; mRNA.
DR   EMBL; AB013394; BAB10242.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95459.1; -; Genomic_DNA.
DR   EMBL; AF360175; AAK25885.1; -; mRNA.
DR   EMBL; AY056349; AAL07198.1; -; mRNA.
DR   RefSeq; NP_199514.1; NM_124074.4.
DR   AlphaFoldDB; Q96252; -.
DR   SMR; Q96252; -.
DR   IntAct; Q96252; 24.
DR   MINT; Q96252; -.
DR   STRING; 3702.AT5G47030.1; -.
DR   PaxDb; Q96252; -.
DR   PRIDE; Q96252; -.
DR   ProteomicsDB; 241062; -.
DR   EnsemblPlants; AT5G47030.1; AT5G47030.1; AT5G47030.
DR   GeneID; 834749; -.
DR   Gramene; AT5G47030.1; AT5G47030.1; AT5G47030.
DR   KEGG; ath:AT5G47030; -.
DR   Araport; AT5G47030; -.
DR   TAIR; locus:2171022; AT5G47030.
DR   eggNOG; KOG1758; Eukaryota.
DR   HOGENOM; CLU_084338_0_2_1; -.
DR   OMA; KVLQQMC; -.
DR   OrthoDB; 1286602at2759; -.
DR   PhylomeDB; Q96252; -.
DR   PRO; PR:Q96252; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q96252; baseline and differential.
DR   Genevisible; Q96252; AT.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; HDA:TAIR.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:11743114"
FT   CHAIN           27..203
FT                   /note="ATP synthase subunit delta', mitochondrial"
FT                   /id="PRO_0000002657"
SQ   SEQUENCE   203 AA;  21548 MW;  ACA68FC72F9DC687 CRC64;
     MFKQASRLLS RSVAAASSKS VTTRAFSTEL PSTLDSTFVE AWKKVAPNMD PPQTPSAFMK
     PRPSTPSSIP TKLTVNFVLP YTSELTGKEV DMVIIPASTG QMGVLPGHVP TIAELKPGIM
     SVHEGTDVKK YFLSSGFAFL HANSVADIIA VEAVPLDHID PSQVQKGLAE FQQKLASATT
     DLEKAEAQIG VEVHSAINAA LSG