ID   ATPG_PEA                Reviewed;         376 AA.
AC   P28552;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=ATP synthase gamma chain, chloroplastic;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Flags: Precursor;
GN   Name=ATPC;
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].
RX   PubMed=1450388; DOI=10.1007/bf00046458;
RA   Napier J.A., Hglund A.S., Plant A.L., Gray J.C.;
RT   "Chloroplast import of the precursor of the gamma subunit of pea
RT   chloroplast ATP synthase.";
RL   Plant Mol. Biol. 20:737-741(1992).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The gamma chain is believed to be important in
CC       regulating ATPase activity and the flow of protons through the CF(0)
CC       complex.
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 four main
CC       subunits: a, b, b' and c (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR   EMBL; X63604; CAA45150.1; -; mRNA.
DR   PIR; S27976; S27976.
DR   AlphaFoldDB; P28552; -.
DR   SMR; P28552; -.
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   CDD; cd12151; F1-ATPase_gamma; 1.
DR   HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
DR   InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR   InterPro; IPR000131; ATP_synth_F1_gsu.
DR   PANTHER; PTHR11693; PTHR11693; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; SSF52943; 1.
DR   TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
PE   2: Evidence at transcript level;
KW   ATP synthesis; CF(1); Chloroplast; Disulfide bond; Hydrogen ion transport;
KW   Ion transport; Membrane; Plastid; Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           53..376
FT                   /note="ATP synthase gamma chain, chloroplastic"
FT                   /id="PRO_0000002678"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000250"
FT   DISULFID        250..256
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41411 MW;  6976834B12F3CD18 CRC64;
     MSCSNVTMLV SSKPSLPDAS NLSFRSAFNP FQLPSQNSSS SCTPSRPTSI QCGLKDLKNR
     IDSVKNTQKI TEAMKLVAAA KVRRAQEAVV NGRPFSETLV EVLYSINEQL QTDDIESPLT
     KLRPVKKVAL VVCTGDRGLC GGFNNAILKK AEARIAELKE LGLEYTVVSV GRKGNSYFNR
     RPYIPVDRFL EGGSLPTAKE AQTIADDVFS LFVSEEVDKV ELLYTKFVSL VKSNPIIHTL
     LPLSPKGEIC DINGNCVDAA EDELFRLTTK EGKLTVERDV IRSKTVDFSP ILQFEQDPVQ
     ILDALLPLYL NSQILRPLQE SLASELAARM SAMSSAFDNA SELKTDLTRV YNRATQAKIT
     GEILEIVAGD IECIIW