ID   ATPG_BRUSU              Reviewed;         292 AA.
AC   Q8FYR4; G0K7D6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
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};
GN   OrderedLocusNames=BR1800, BS1330_I1794;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30695.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM19112.1; -; Genomic_DNA.
DR   RefSeq; WP_004689233.1; NZ_KN046804.1.
DR   AlphaFoldDB; Q8FYR4; -.
DR   SMR; Q8FYR4; -.
DR   GeneID; 58775211; -.
DR   KEGG; bms:BR1800; -.
DR   KEGG; bsi:BS1330_I1794; -.
DR   PATRIC; fig|204722.21.peg.1183; -.
DR   HOGENOM; CLU_050669_0_1_5; -.
DR   PhylomeDB; Q8FYR4; -.
DR   Proteomes; UP000007104; Chromosome I.
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   Gene3D; 3.40.1380.10; -; 1.
DR   Gene3D; 1.10.287.80; ATP synthase, gamma subunit, helix hairpin domain; 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   NCBIfam; TIGR01146; ATPsyn_F1gamma; 1.
DR   PANTHER; PTHR11693; ATP SYNTHASE GAMMA CHAIN; 1.
DR   PANTHER; PTHR11693:SF41; ATP SYNTHASE GAMMA CHAIN 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PIRSF; PIRSF039089; ATP_synthase_gamma; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; ATP synthase (F1-ATPase), gamma subunit; 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..292
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073251"
SQ   SEQUENCE   292 AA;  31813 MW;  0C33716BC41EA04F CRC64;
     MPSLKDLRNR IASVKATQKI TKAMQMVAAA KLRRAQEAAE AARPYSQRMG AVLANIAQNV
     SGEDAPALMV GTGKDDVHLL VVCTAERGLC GGFNSQIARL ARDHARKLLA EGKTVKIITV
     GKKGADILRR EFSALLHDHV DLREVKQLAF VHADQIGHKI IKLFEEGAFD VCTLFYSEFK
     SVISQVPTAQ QLIPASADNE AEMETAGDAI YEYEPDPAAI LSTLIPRNIS VQIFRALLEN
     VAGEMGAKMS AMDNATRNAG DMINKLSITY NRQRQAQITK ELIEIISGAE AL
//