ID   ATPG_STRR6              Reviewed;         292 AA.
AC   Q7CRB2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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}; OrderedLocusNames=spr1361;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=11580837; DOI=10.1046/j.1365-2958.2001.02597.x;
RA   Martin-Galiano A.J., Ferrandiz M.J., de la Campa A.G.;
RT   "The promoter of the operon encoding the F0F1 ATPase of Streptococcus
RT   pneumoniae is inducible by pH.";
RL   Mol. Microbiol. 41:1327-1338(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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:0000255|HAMAP-Rule:MF_00815,
CC       ECO:0000269|PubMed:11580837}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11580837};
CC       Peripheral membrane protein {ECO:0000305|PubMed:11580837}.
CC   -!- INDUCTION: Induced by a decrease in external pH from 7.5 to 5.7.
CC       {ECO:0000269|PubMed:11580837}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR   EMBL; AF368465; AAL66418.1; -; Genomic_DNA.
DR   EMBL; AE007317; AAL00165.1; -; Genomic_DNA.
DR   RefSeq; NP_358954.1; NC_003098.1.
DR   RefSeq; WP_000301212.1; NC_003098.1.
DR   AlphaFoldDB; Q7CRB2; -.
DR   SMR; Q7CRB2; -.
DR   STRING; 171101.spr1361; -.
DR   EnsemblBacteria; AAL00165; AAL00165; spr1361.
DR   GeneID; 60233439; -.
DR   KEGG; spr:spr1361; -.
DR   PATRIC; fig|171101.6.peg.1475; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_9; -.
DR   OMA; MQITSAM; -.
DR   Proteomes; UP000000586; 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); IBA:GO_Central.
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:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..292
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073388"
SQ   SEQUENCE   292 AA;  32325 MW;  B5D80482B6EDDBC4 CRC64;
     MAVSLNDIKT KIASTKNTSQ ITNAMQMVSA AKLGRSEEAA RNFQVYAQKV RKLLTDILHG
     NGAGASTNPM LISRSVKKTG YIVITSDRGL VGGYNSSILK AVMELKEEYH PDGKGFEMIC
     IGGMGADFFK ARGIQPLYEL RGLSDQPSFD QVRKIISKTV EMYQNELFDE LYVCYNHHVN
     TLTSQMRVEQ MLPIVDLDPN EADEEYSLTF ELETSREEIL EQLLPQFAES MIYGAIIDAK
     TAENAAGMTA MQTATDNAKK VINDLTIQYN RARQAAITQE ITEIVAGASA LE