ID   ATPG_OENOE              Reviewed;         303 AA.
AC   Q8KM29;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
OS   Oenococcus oeni (Leuconostoc oenos).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=1247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E656;
RX   PubMed=14529177; DOI=10.1078/072320203322497374;
RA   Sievers M., Uermoesi C., Fehlmann M., Krieger S.;
RT   "Cloning, sequence analysis and expression of the F1F0-ATPase beta-subunit
RT   from wine lactic acid bacteria.";
RL   Syst. Appl. Microbiol. 26:350-356(2003).
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: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00815};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; AJ430065; CAD22546.1; -; Genomic_DNA.
DR   RefSeq; WP_002818533.1; NZ_QYTB01000010.1.
DR   AlphaFoldDB; Q8KM29; -.
DR   SMR; Q8KM29; -.
DR   PATRIC; fig|1247.145.peg.1736; -.
DR   OMA; MQITSAM; -.
DR   GO; GO:0005886; C:plasma 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   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; 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   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   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Transport.
FT   CHAIN           1..303
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073333"
SQ   SEQUENCE   303 AA;  33794 MW;  53636DC53853210A CRC64;
     MASLQDIRRR IDSTKKTSQI TSAMQMVSSS KLIQIQKHTS GYLDYANHVE AIVAHLAAAH
     LLEHQNGSSI PFITQRPVKT TAILVITSDR GLVGGYNNQV LKRTDQIMRE QKLTKENAVI
     FALGGKGSDY YAKRGFTIAF ENRDITDVPK FWEVSDLVKE VTKQYAARKF DALELVFNHF
     INRLKNDVVN QQILPIRSEN FQRDEKGNLT ADKYKGQSSI YEFEPAPESL LKIVLPQFAQ
     SLLYGAILDA KTAEHAASAS AMRAATDNAK DLISTLELKY NRARQAAITT EITEITGGMA
     ALQ