ID   ATPG_ALIB4              Reviewed;         295 AA.
AC   A8EV71;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Abu_1596;
OS   Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Aliarcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018;
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA   Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the Epsilonproteobacterium
RT   Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV67844.1; -; Genomic_DNA.
DR   RefSeq; WP_012147588.1; NC_009850.1.
DR   AlphaFoldDB; A8EV71; -.
DR   SMR; A8EV71; -.
DR   STRING; 367737.Abu_1596; -.
DR   PRIDE; A8EV71; -.
DR   EnsemblBacteria; ABV67844; ABV67844; Abu_1596.
DR   GeneID; 56463784; -.
DR   KEGG; abu:Abu_1596; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_7; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 1701531at2; -.
DR   Proteomes; UP000001136; 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   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.
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..295
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_1000062288"
SQ   SEQUENCE   295 AA;  32899 MW;  6304C959120AA116 CRC64;
     MANLKEIKLK IGSVKNTQKT TKAMKLVSSA KLTRTRQLSE QARSYAHKIN DVLSDIAARV
     SKVQDDGNIG RSFLQNDNPK TVDIVFVTAD KGLCGGFNMA TIKTVSRLIS EYEAKGTKVR
     LRAAGRKGVD FFSFQGMTIE QKATDLSSAP DYDRAAEFIH NVVEDFKNEV TDKVVIVYNG
     FLNMLSQEIR VRDLLPISLD DVKIQDNASM LNIEPEEDED EVLNELTDKY IDFNMYYALI
     DSLAAEHSAR MQAMEAASKN AKEKVNSLTV EYNKARQAAI TTELIEIISG VEALK