ID   ATPG_STRLI              Reviewed;         303 AA.
AC   P50007;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
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};
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC   STRAIN=66 / 1326;
RX   PubMed=7828915; DOI=10.1016/0378-1119(95)00673-t;
RA   Hensel M., Lill H., Schmid R., Deckers-Hebestreit G., Altendorf K.;
RT   "The ATP synthase (F1F0) of Streptomyces lividans: sequencing of the atp
RT   operon and phylogenetic considerations with subunit beta.";
RL   Gene 152:11-17(1995).
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; Z22606; CAA80326.1; -; Genomic_DNA.
DR   PIR; S37546; S37546.
DR   AlphaFoldDB; P50007; -.
DR   SMR; P50007; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7828915"
FT   CHAIN           2..303
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073400"
SQ   SEQUENCE   303 AA;  32871 MW;  0FEAEC00BF07EF21 CRC64;
     MGAQLRVYKR RIRSVTATKK ITKAMEMIAA SRVVKAQRKV AASTPYAREL TLPRLGTGSN
     TKHPLTTEAD SPSRAAVLLL TSDRGLAGAF NSNSIKAAEQ LTERLEREGR QVDTYIVGRR
     GLAHYNFRER KVVESFAGFT DEPTYADAKK VAAPLIEAIE KDTAEGGVDE LHIVYTEFVS
     MMTQTAVDSR LLPLSLDEVA EESGAKDEIL PLYDFEPSAE DVLDALLPRY VESRIYNALL
     QSAASKHAAT RRAMKSATDN AGELINTLSR LANAARQAEI TQEISEIVGG ASALADANAG
     SDN