ID   ATPG_PELUB              Reviewed;         291 AA.
AC   Q4FP37;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}; OrderedLocusNames=SAR11_0231;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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 inner 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; CP000084; AAZ21052.1; -; Genomic_DNA.
DR   RefSeq; WP_011281555.1; NC_007205.1.
DR   AlphaFoldDB; Q4FP37; -.
DR   SMR; Q4FP37; -.
DR   STRING; 335992.SAR11_0231; -.
DR   PRIDE; Q4FP37; -.
DR   EnsemblBacteria; AAZ21052; AAZ21052; SAR11_0231.
DR   GeneID; 66294728; -.
DR   KEGG; pub:SAR11_0231; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_5; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 1701531at2; -.
DR   Proteomes; UP000002528; Chromosome.
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 inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..291
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073336"
SQ   SEQUENCE   291 AA;  32688 MW;  0C4BA5D52A1EADF8 CRC64;
     MATLDDLKKR IASVKSTQKI TKAMKMVAAA KLRRAQENAE KGRPYSEKMN NIILNLSSGI
     SDKENAPKLL SGTGEDKVHL CIVLTSDRGL CGGFNTNIIK KAKTYFQKIS DEGKTLKIIT
     VGSKGYDQLK RVYKDAIVER ISFKDSKTIN YLDAEKVGKM IIENFEKEEF DVCTIFYNKF
     KNVITQIPQE QQIIPLKTSE AEENSSEDNY EFEPDEDEIL SNLLPKNIST QIFKAMLENS
     ASEQGSRMSA MDNATRNAGE MVDKLTIEYN RSRQAAITKE LIEIISGAES L