ID   ATPD_SORBI              Reviewed;         247 AA.
AC   Q07300;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=ATP synthase delta chain, chloroplastic;
DE   AltName: Full=F-ATPase delta chain;
DE   Flags: Precursor;
GN   Name=ATPD; OrderedLocusNames=Sb03g017580;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8481382; DOI=10.1016/0005-2728(93)90157-b;
RA   Hoesche J.A., Berzborn R.J.;
RT   "Primary structure, deduced from cDNA, secondary structure analysis and
RT   conclusions concerning interaction surfaces of the delta subunit of the
RT   photosynthetic ATP-synthase (E.C. 3.6.3.14) from millet (Sorghum bicolor)
RT   and maize (Zea mays).";
RL   Biochim. Biophys. Acta 1142:293-305(1993).
CC   -!- FUNCTION: This protein seems to be part of the stalk that links CF(0)
CC       to CF(1). It either transmits conformational changes from CF(0) into
CC       CF(1) or is implicated in proton conduction.
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: Plastid, chloroplast thylakoid membrane.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR   EMBL; X66004; CAA46803.1; -; mRNA.
DR   PIR; S43728; S43728.
DR   RefSeq; XP_002454273.1; XM_002454228.1.
DR   AlphaFoldDB; Q07300; -.
DR   SMR; Q07300; -.
DR   STRING; 4558.Sb04g027810.1; -.
DR   EnsemblPlants; EES07249; EES07249; SORBI_3004G235200.
DR   GeneID; 8066424; -.
DR   Gramene; EES07249; EES07249; SORBI_3004G235200.
DR   KEGG; sbi:8066424; -.
DR   eggNOG; KOG1662; Eukaryota.
DR   HOGENOM; CLU_085114_1_0_1; -.
DR   OMA; QVIVAHE; -.
DR   OrthoDB; 1432799at2759; -.
DR   ExpressionAtlas; Q07300; baseline and differential.
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:0010319; C:stromule; IEA:EnsemblPlants.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IEA:EnsemblPlants.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:EnsemblPlants.
DR   GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
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; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   PANTHER; PTHR11910; PTHR11910; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; SSF47928; 1.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   2: Evidence at transcript level;
KW   ATP synthesis; CF(1); Chloroplast; Hydrogen ion transport; Ion transport;
KW   Membrane; Plastid; Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..60
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           61..247
FT                   /note="ATP synthase delta chain, chloroplastic"
FT                   /id="PRO_0000002640"
SQ   SEQUENCE   247 AA;  26736 MW;  ABE877BEA32D21AC CRC64;
     MAALRLASFT LRPAAAAAAS ASSGATPAAP RSASFARAAR GLPSLRLAPP RRRGDLVRPR
     AEAAADSYAS ALSEVAVENG TLEQTVSDLE KLQKIFADET VAEFFDNPTV PREEKTALID
     EIAKSYELQP HVVNFINVVV DNFRATILPE IVVEFENIFN SLTGTEVATV TSVVQLESQD
     LAQIAQHVQK MTGAKNVRLK TQLDPELIAG FTVQYGRDGS SLIDMSVRKQ IEEITSEFEL
     PDVPLEV