ID   ATPG_VIBAL              Reviewed;         288 AA.
AC   P12990;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 100.
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}; Synonyms=uncG;
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=138-2;
RX   PubMed=2529481; DOI=10.1093/nar/17.19.7993;
RA   Krumholz L.R., Esser U., Simoni R.D.;
RT   "Nucleotide sequence of the unc operon of Vibrio alginolyticus.";
RL   Nucleic Acids Res. 17:7993-7994(1989).
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; X16050; CAA34180.1; -; Genomic_DNA.
DR   PIR; S06081; S06081.
DR   AlphaFoldDB; P12990; -.
DR   SMR; P12990; -.
DR   STRING; 663.BAU10_15085; -.
DR   PRIDE; P12990; -.
DR   eggNOG; COG0224; Bacteria.
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; Transport.
FT   CHAIN           1..288
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073410"
SQ   SEQUENCE   288 AA;  31890 MW;  BD612B584AC0B7BB CRC64;
     MAGAKEIRNK IGSVKSTQKI TKAMEMVAAS KMRRSQDAME ASRPYAETMR KVIGHVANAN
     LEYRHPYLEE REAKRVGYII VSTDRGLCGG LNINVFKKAV TDMQTWREKG AEIELAVVGS
     KATAFFKHGG AKVAAQVSGL GDNPSLEDLI GSVGVMLKKY DEGELDRLYV VFNKFVNTMV
     QQPTIDQLLP LPKSDSEEMQ REHSWDYIYE PEPKPLLDTL LVRYVESQVY QGVVENLACE
     QAARMIAMKA ATDNATNLID DLELVYNKAR QAAITQELSE IVGGAAAV