ID   ATPG_BACP3              Reviewed;         286 AA.
AC   P09222;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=ATP synthase gamma chain;
DE   AltName: Full=ATP synthase F1 sector gamma subunit;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Flags: Precursor;
GN   Name=atpG;
OS   Bacillus sp. (strain PS3).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 5-19, AND SUBUNIT.
RX   PubMed=2894854; DOI=10.1016/0005-2728(88)90064-3;
RA   Ohta S., Yohda M., Ishizuka M., Hirata H., Hamamoto T.,
RA   Otawara-Hamamoto Y., Matsuda K., Kagawa Y.;
RT   "Sequence and over-expression of subunits of adenosine triphosphate
RT   synthase in thermophilic bacterium PS3.";
RL   Biochim. Biophys. Acta 933:141-155(1988).
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.
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:0000269|PubMed:2894854}.
CC   -!- INTERACTION:
CC       P09222; P07677: atpD; NbExp=2; IntAct=EBI-15654225, EBI-8612954;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR   EMBL; X07804; CAA30653.1; -; Genomic_DNA.
DR   AlphaFoldDB; P09222; -.
DR   BMRB; P09222; -.
DR   SMR; P09222; -.
DR   DIP; DIP-29622N; -.
DR   IntAct; P09222; 1.
DR   TCDB; 3.A.2.1.14; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
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   1: Evidence at protein level;
KW   ATP synthesis; Cell membrane; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Transport.
FT   PROPEP          1..4
FT                   /evidence="ECO:0000269|PubMed:2894854"
FT                   /id="PRO_0000002672"
FT   CHAIN           5..286
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000002673"
SQ   SEQUENCE   286 AA;  32248 MW;  A8B96F687C999252 CRC64;
     MKPLASLRDI KTRINATKKT SQITKAMEMV LTSKLNRAEK REIVRPYMEK IQEVVANVAL
     AARASHPMLV SRPVKKTGYL VITSDRGLAG AYNSNVLRLV YQTIQKRHAS PDEYAIIVIG
     RVGLSFFRKR NMPVILDITR LPDQPSFADI KEIARKTVGL FADGTFDELY MYYNHYVSAI
     QQEVTERKLL PLTDLAENKQ RTVYEFEPSQ EEILDVLLPQ YAESLIYGAL LDAKASEHAA
     RMTAMKNATD NANELIRTLT LSYNRARQAA ITQEITEIVA GANALQ