ID   ATPG_ARTPT              Reviewed;         311 AA.
AC   P50006;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=ATP synthase gamma chain;
DE   AltName: Full=ATP synthase F1 sector gamma subunit;
DE   AltName: Full=F-ATPase gamma subunit;
GN   Name=atpG; Synonyms=atpC;
OS   Arthrospira platensis (Spirulina platensis).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Arthrospira.
OX   NCBI_TaxID=118562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC   STRAIN=C1;
RX   PubMed=7612646; DOI=10.1016/0005-2728(95)00052-k;
RA   Steinemann D., Lill H.;
RT   "Sequence of the gamma-subunit of Spirulina platensis: a new principle of
RT   thiol modulation of F0F1 ATP synthase?";
RL   Biochim. Biophys. Acta 1230:86-90(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 (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Thiol-modulation by raising the activation
CC       threshold of the enzyme upon oxidation of the cysteines, thereby
CC       preventing wasteful ATP-hydrolysis.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR   EMBL; Z46799; CAA86820.1; -; Genomic_DNA.
DR   PIR; S49845; S49845.
DR   AlphaFoldDB; P50006; -.
DR   SMR; P50006; -.
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   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.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Disulfide bond;
KW   Hydrogen ion transport; Ion transport; Membrane; Thylakoid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7612646"
FT   CHAIN           2..311
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073372"
FT   DISULFID        67..138
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   311 AA;  34492 MW;  8E13DBC09F21C572 CRC64;
     MSNLKAIRDR IQSVKNTKKI TEAMRLVASA KVRRAQEQVL ATRPFADRLA GVLYGLQGRL
     QFEDVECPLL QQREVKKVGL VVLAGNRGLC GAYNSNIIKR AEARAAELKA EGLEYSYLLV
     GRKAIQHFTR RDAPISQCRD NPEKTPDPQE VSSATDEILA WFESGAVDRV ELIYTKFVSL
     ISSRPVTQTL LPLDLQGLEA QDDEVFRLTS KGGKFDVTRE KVSVEPEALA QDMIFEQDPV
     EILNALLPLF LTNQLLRAWQ ESTASELAAR MTAMSNASDN ASDLVKTLTL SYNKARQASI
     TQELLEVVAG A