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ATPG_TRIEI
ID   ATPG_TRIEI              Reviewed;         314 AA.
AC   Q112Z7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Tery_2198;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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: Cellular thylakoid 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; CP000393; ABG51427.1; -; Genomic_DNA.
DR   RefSeq; WP_011611796.1; NC_008312.1.
DR   AlphaFoldDB; Q112Z7; -.
DR   SMR; Q112Z7; -.
DR   STRING; 203124.Tery_2198; -.
DR   PRIDE; Q112Z7; -.
DR   EnsemblBacteria; ABG51427; ABG51427; Tery_2198.
DR   KEGG; ter:Tery_2198; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_0_3; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 1701531at2; -.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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   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; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Thylakoid; Transport.
FT   CHAIN           1..314
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_1000053372"
SQ   SEQUENCE   314 AA;  34823 MW;  E828466FE28D5C43 CRC64;
     MPNLKAIRDR IKSIKNTKKI TEAMRLVAAA KVRRAQEQVI GTRPFADRLA QVLYGLAERL
     QFESLDLPLL QKREAKTVGL LVISGNRGLC GSYNTNVIKR AEMRARELTQ QGINCQYVLI
     GRKAIQYFQR REVPILNTYD NPEKIPTADN ASVVADEILA GFMAGSIDRV ELIFTRFISL
     ISSKPVIQTL LPLDPQGLEV KDDEIFRLTS KGGEFEVSRE TVSAAVKSFP RDMIFEQDPI
     QILDALLPLF LTNQLLRAWQ ESSASELASR MTAMSNASDN ASELAGTLTL AYNKARQAAI
     TQEILEVVGG ANAL
 
 
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