ID   ATPG_ACIFI              Reviewed;         298 AA.
AC   P41169;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
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   Acidithiobacillus ferridurans.
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=1232575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX   PubMed=7958772; DOI=10.1111/j.1574-6968.1994.tb07137.x;
RA   Brown L.D., Dennehy M.E., Rawlings D.E.;
RT   "The F1 genes of the F1F0 ATP synthase from the acidophilic bacterium
RT   Thiobacillus ferrooxidans complement Escherichia coli F1 unc mutants.";
RL   FEMS Microbiol. Lett. 122:19-26(1994).
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; M81087; AAA53126.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41169; -.
DR   SMR; P41169; -.
DR   STRING; 380394.Lferr_2808; -.
DR   PRIDE; P41169; -.
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..298
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073408"
SQ   SEQUENCE   298 AA;  33318 MW;  D798B13068548540 CRC64;
     MANAKEIRGQ IKSVKNTRKI TRAMEMVAAS KMRRAQERMR AARPCAEKIR EVLGHLAQAH
     PEYEHPLMQV RPVKKAGFLV VTTDRGLCGG LNVNVLRNVV QKMRELHEEG VESNLAVVGN
     KGLGFLRRHG AHLVADVNGL GDSPHLGDMI GPIRAMADAY AKGEVDVVYL VSSRFVNTML
     QRATVEQLLP VEKPTASAEQ RAELWDYIYE PEARPVLDRL MQRYVESVVY QAVIEHLACE
     QSARMVAMKS ASDNAKRMVD DLQLAYNKAR QAAITQEIAE ISAGAARFDD CAQHFWKF