ID   ATPG_TRICV              Reviewed;         370 AA.
AC   Q06908;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=ATP synthase gamma chain, chloroplastic;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Flags: Precursor;
GN   Name=ATPC;
OS   Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC   Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX   NCBI_TaxID=1514140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8462677; DOI=10.1016/0014-5793(93)81658-m;
RA   Pancic P.G., Strotmann H.;
RT   "Structure of the nuclear encoded gamma subunit of CF0CF1 of the diatom
RT   Odontella sinensis including its presequence.";
RL   FEBS Lett. 320:61-66(1993).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X70650; CAA49993.1; -; mRNA.
DR   PIR; S32401; S32401.
DR   AlphaFoldDB; Q06908; -.
DR   SMR; Q06908; -.
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   InterPro; IPR023632; ATP_synth_F1_gsu_CS.
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.
DR   PROSITE; PS00153; ATPASE_GAMMA; 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..55
FT                   /note="Chloroplast"
FT   CHAIN           56..370
FT                   /note="ATP synthase gamma chain, chloroplastic"
FT                   /id="PRO_0000002677"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  40133 MW;  CE367969CC940F93 CRC64;
     MKFFCVAGLL ASAAAFQAQP AAFTTYSPAV GGATSNVFSE SSSPAHRNRR ATIVMDGKAN
     AIRDRITSVK NTKKITMAMK LVAAAKVRRA QDAVLATRPF SETLQSVFGG LIARMGGEAL
     DLPLLTQREV SKVTLVVITG DRGLCGGYNS FMIKKAEARF NELKDQGVAC DMVLIGKKGI
     TYFQRRGYPI RKTFETGQNP DSKQALAISE ELLNTYLSGE SDAVELLYTK FISLIASSPS
     ARTLIPFSAS EITQQGDEVF QLTSSGGDFE VERTELEVAE PQDFPNDMIF EQDPIQIINS
     ILPLYLNGQI LRTLQESVAS ELAARMQSMQ SASDNAGDLA KRLSTEYNRA RQAAVTQEIL
     EIVSGASALE