ID   ATPD_HETA4              Reviewed;         203 AA.
AC   B2XTP5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=ATP synthase subunit delta, chloroplastic {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};
GN   Name=atpD {ECO:0000255|HAMAP-Rule:MF_01416};
GN   OrderedLocusNames=Heak452_Cp080;
OS   Heterosigma akashiwo (strain CCMP452 / OLISTH).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Raphidophyceae; Chattonellales;
OC   Chattonellaceae; Heterosigma.
OX   NCBI_TaxID=536046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18462506; DOI=10.1186/1471-2164-9-211;
RA   Cattolico R.A., Jacobs M.A., Zhou Y., Chang J., Duplessis M., Lybrand T.,
RA   McKay J., Ong H.C., Sims E., Rocap G.;
RT   "Chloroplast genome sequencing analysis of Heterosigma akashiwo CCMP452
RT   (West Atlantic) and NIES293 (West Pacific) strains.";
RL   BMC Genomics 9:211-211(2008).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01416}.
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. {ECO:0000255|HAMAP-Rule:MF_01416}.
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). CF(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is 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, b and b'
CC       chains. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01416}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR   EMBL; EU168191; ABV70128.1; -; Genomic_DNA.
DR   RefSeq; YP_001936381.1; NC_010772.1.
DR   AlphaFoldDB; B2XTP5; -.
DR   SMR; B2XTP5; -.
DR   GeneID; 6335679; -.
DR   GO; GO:0009535; C:chloroplast thylakoid 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:UniProtKB-UniRule.
DR   Gene3D; 1.10.520.20; -; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   PANTHER; PTHR11910; PTHR11910; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   SUPFAM; SSF47928; SSF47928; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(1); Chloroplast; Hydrogen ion transport; Ion transport;
KW   Membrane; Plastid; Thylakoid; Transport.
FT   CHAIN           1..203
FT                   /note="ATP synthase subunit delta, chloroplastic"
FT                   /id="PRO_0000371214"
SQ   SEQUENCE   203 AA;  23059 MW;  624E7DECA41D5743 CRC64;
     MSTNSRAGDA YAYALLKVLF NETKDFDSFS DLVGDVLDFV TIFNTCPSIE EFFANPTYSP
     IQKKQFLYDF FGRSLNPILM SFLYLLCDTK RIIYISSIIS IFLETLLKNT NSHIVEVQTP
     TGKDYKLDIS KLETTLSGWF NKIQKNNDEA VNFLNFDESL VIFTVKEVPG LLGGFRLNFV
     TDSKVIDFSI AGKIKRLAAV LNY