ID   ATPG_STRSA              Reviewed;         293 AA.
AC   Q9ZJ02;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Streptococcus sanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=10904;
RX   PubMed=12591869; DOI=10.1128/jb.185.5.1525-1533.2003;
RA   Kuhnert W.L., Quivey R.G. Jr.;
RT   "Genetic and biochemical characterization of the F-ATPase operon from
RT   Streptococcus sanguis 10904.";
RL   J. Bacteriol. 185:1525-1533(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; AF001955; AAD00917.1; -; Genomic_DNA.
DR   RefSeq; WP_002895995.1; NZ_RQZI01000005.1.
DR   AlphaFoldDB; Q9ZJ02; -.
DR   SMR; Q9ZJ02; -.
DR   GeneID; 61536084; -.
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   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; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Transport.
FT   CHAIN           1..293
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073394"
SQ   SEQUENCE   293 AA;  32541 MW;  546D2F7A86898485 CRC64;
     MAVSLNDIKN KIASTKNTSQ ITNAMQMVSA AKLGKSEEAA KNFQVYAQKV RKLVTDMLHG
     HEAENARHHS MLISRPVKKS AYIVITSDRG LVGGYNATIL KALMELKAEY HPTGEDFEVI
     CIGSVGADFF RARGIQPVYE LRGLADQPSF DEVRKIISKT IEMYQNELFD ELYVCYNHHV
     NSLTSQMRVE QMLPIIDLDP NEADEDYTLN LELESSRDSI LDQLLPQFAE SMIYGAIIDA
     KTAENAAGMT AMQTATDNAK KVISDLTIQY NRARQAAITQ EITEIVAGAS ALE