ID   ATPD_PEA                Reviewed;         251 AA.
AC   Q02758;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=ATP synthase delta chain, chloroplastic;
DE   AltName: Full=F-ATPase delta chain;
DE   Flags: Precursor;
GN   Name=ATPD;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 65-251.
RX   PubMed=1482682; DOI=10.1016/0167-4781(92)90121-f;
RA   Hoesche J.A., Berzborn R.J.;
RT   "Cloning and sequencing of a cDNA for the delta-subunit of photosynthetic
RT   ATP-synthase (EC 3.6.3.14) from pea (Pisum sativum).";
RL   Biochim. Biophys. Acta 1171:201-204(1992).
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; M94558; AAA33647.1; -; mRNA.
DR   PIR; S28171; S28171.
DR   AlphaFoldDB; Q02758; -.
DR   SMR; Q02758; -.
DR   EnsemblPlants; Psat4g066200.1; Psat4g066200.1.cds; Psat4g066200.
DR   Gramene; Psat4g066200.1; Psat4g066200.1.cds; Psat4g066200.
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:InterPro.
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   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Chloroplast; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Plastid; Thylakoid;
KW   Transit peptide; Transport.
FT   TRANSIT         1..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:1482682"
FT   CHAIN           65..251
FT                   /note="ATP synthase delta chain, chloroplastic"
FT                   /id="PRO_0000002639"
SQ   SEQUENCE   251 AA;  27624 MW;  CD74B4CA16658B6C CRC64;
     MASLQHTTAS LHSKHIPKTT NILTRKPILN LSSSTFYSPK LKLKLKLPLT KTRRSTGGAL
     GARMSSLAAG SYAAALADLA NSNNTLDAIT ADFDKIEQLF SDPKVFDYFS SPIVEDSTKR
     QLIGEFATTS GFQPHTHNFL NVLIDSKRID MIIDIIKEFE FVYNTLTDTE LVVVTSVVKL
     ESHHLAQIAK QVQKLTGAKK VRTKTLLDPS LVAGFTVRYG NTGSKFIDMS VKRKLEEIAA
     QIDLGDIQLA V