ID   ATPG_STRMU              Reviewed;         292 AA.
AC   P95788;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 126.
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   Synonyms=atpC {ECO:0000255|HAMAP-Rule:MF_00815};
GN   OrderedLocusNames=SMU_1529;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=8996091; DOI=10.1016/s0378-1119(96)00502-1;
RA   Smith A.J., Quivey R.G., Faustoferri R.C.;
RT   "Cloning and nucleotide sequence analysis of the Streptococcus mutans
RT   membrane-bound, proton-translocating ATPase operon.";
RL   Gene 183:87-96(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00815};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; U31170; AAD13382.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59179.1; -; Genomic_DNA.
DR   PIR; JC5740; JC5740.
DR   RefSeq; NP_721873.1; NC_004350.2.
DR   RefSeq; WP_002262941.1; NC_004350.2.
DR   AlphaFoldDB; P95788; -.
DR   SMR; P95788; -.
DR   STRING; 210007.SMU_1529; -.
DR   PRIDE; P95788; -.
DR   EnsemblBacteria; AAN59179; AAN59179; SMU_1529.
DR   GeneID; 66819080; -.
DR   KEGG; smu:SMU_1529; -.
DR   PATRIC; fig|210007.7.peg.1361; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_9; -.
DR   OMA; MQITSAM; -.
DR   PhylomeDB; P95788; -.
DR   SABIO-RK; P95788; -.
DR   Proteomes; UP000002512; 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   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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..292
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073386"
FT   CONFLICT        56
FT                   /note="D -> H (in Ref. 1; AAD13382)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="R -> H (in Ref. 1; AAD13382)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   292 AA;  32349 MW;  5BF292A6ACD38BB9 CRC64;
     MTGSLSEIKV RITSTQKTGK ITSAMKMVSS AKLVKSEQAA KDFQIYASKI RQITTDLLHS
     DLRKGSSNPM LISRPIKKTA YIVITSDKGL VGAYNSTILK AVMDTIKDYH PKGDDYTIIS
     IGGMGSDFFR ARHIPVAFEL RGLEDNPSFE EVNRIISKSV EMYKNELFDE LYVCYSHHIN
     SLTSQVRVEK MLPISDLDAD EASEDNVANF ELEPSREAIL EQLLPQYAES LIYGAIIDAK
     TAEHAAGMTA MQTATDNADK VIEDLTKLYN RVRQAAITQE ITEIVAGANA LD