ID   ATPG_SYNP1              Reviewed;         315 AA.
AC   Q05384;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815};
DE   AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
DE   AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
GN   Name=atpG {ECO:0000255|HAMAP-Rule:MF_00815};
GN   Synonyms=atpC {ECO:0000255|HAMAP-Rule:MF_00815};
OS   Synechococcus sp. (strain PCC 6716).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32048;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8363578; DOI=10.1042/bj2940239;
RA   van Walraven H.S., Lutter R., Walker J.E.;
RT   "Organization and sequences of genes for the subunits of ATP synthase in
RT   the thermophilic cyanobacterium Synechococcus 6716.";
RL   Biochem. J. 294:239-251(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. {ECO:0000255|HAMAP-Rule:MF_00815}.
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. {ECO:0000255|HAMAP-Rule:MF_00815}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00815}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR   EMBL; X70433; CAA49889.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05384; -.
DR   SMR; Q05384; -.
DR   GO; GO:0031676; C:plasma membrane-derived 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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Thylakoid; Transport.
FT   CHAIN           1..315
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073404"
SQ   SEQUENCE   315 AA;  34942 MW;  025AB2BAAC469A77 CRC64;
     MPNLKAIRDR IKTIKDTRKI TEAMRLVAAA KVRRAQEQVM ASRPFADRLA QVLYGLQTRL
     RFEDANLPLL AKRPVKTVAL LVVTGDRGLC GGYNTNVIRR AKERTEELEA EGIKYTLVIV
     GRKAAQYFQR RDYPIDAVYS GLEQIPSASE AGQIANELLS LFLSETVDRV ELIYTKFVSL
     ISSKPVVQTL LPLDPQGLEA ADDEIFRLTT RASHLEVNRE KVTSNLPALP PDMIFEQDPV
     QILDALLPLY LSNQLLRALQ EAAASELAAR MTAMNNASDN AQTLIGTLTL SYNKARQAAI
     TQEILEVVAG AEALR