ID   ATP4_IPOBA              Reviewed;         200 AA.
AC   Q40089;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=ATP synthase subunit delta', mitochondrial;
DE   AltName: Full=F-ATPase delta' subunit;
DE   Flags: Precursor;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1370454; DOI=10.1016/s0021-9258(18)48460-8;
RA   Morikame A., Aiso K., Asahi T., Nakamura K.;
RT   "The delta'-subunit of higher plant six-subunit mitochondrial F1-ATPase is
RT   homologous to the delta-subunit of animal mitochondrial F1-ATPase.";
RL   J. Biol. Chem. 267:72-76(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-56.
RX   PubMed=2536736; DOI=10.1016/s0021-9258(18)94048-2;
RA   Kimura T., Nakamura K., Kajiura H., Hattori H., Nelson N., Asahi T.;
RT   "Correspondence of minor subunits of plant mitochondrial F1ATPase to
RT   F1F0ATPase subunits of other organisms.";
RL   J. Biol. Chem. 264:3183-3186(1989).
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; D10660; BAA01511.1; -; mRNA.
DR   PIR; A41740; A41740.
DR   AlphaFoldDB; Q40089; -.
DR   SMR; Q40089; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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   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   Transit peptide; Transport.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2536736"
FT   CHAIN           22..200
FT                   /note="ATP synthase subunit delta', mitochondrial"
FT                   /id="PRO_0000002658"
SQ   SEQUENCE   200 AA;  21318 MW;  1563325C81BCE828 CRC64;
     MFRHSSRLLA RATTMGWRRP FSTDLPAETA ADSTFVEAWK KLIPNVDPPK TPSAYMAPRP
     ATPSSIPSKL TVNFVLPYSS ELAGKEVDMV IIPATTGQMG VLPGHVATIA ELKPGVMSVH
     EGNDVSKYFV SGGFAFIHAN SFADIIAVEA VPLDRIDANL VQKGLAEFTQ KLNTASTDVE
     KAEAQIGVDV HSALNAALTG