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ATPG_PROM2
ID   ATPG_PROM2              Reviewed;         316 AA.
AC   A8G6V0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=P9215_17181;
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000825; ABV51331.1; -; Genomic_DNA.
DR   RefSeq; WP_012008353.1; NC_009840.1.
DR   AlphaFoldDB; A8G6V0; -.
DR   SMR; A8G6V0; -.
DR   STRING; 93060.P9215_17181; -.
DR   EnsemblBacteria; ABV51331; ABV51331; P9215_17181.
DR   KEGG; pmh:P9215_17181; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_0_3; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 1701531at2; -.
DR   Proteomes; UP000002014; Chromosome.
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   3: Inferred from homology;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Thylakoid; Transport.
FT   CHAIN           1..316
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_1000062293"
SQ   SEQUENCE   316 AA;  35345 MW;  D1CFBF825BF6C475 CRC64;
     MANLKEIRDR IVSVKNTRKI TEAMRLVAAA KVRRAQDQVL KSRPFADKLA RVLENIQSRV
     QFEAVDSPLL SKREVKSISL VCITADRGLC GGYNTNIIKK VEIRYAELVK QGFQPNLILV
     GKKAIGFFQN RKDRYVIKST FKELEQVPTV KDSEGITNEI LAEFLSENSD RVEIIYTKFI
     TLVSCAPVVQ TLLPLDPQGI AEENDEIFRL TTKDSKLLVE KSNIEKSDSE KLPSDIVFEQ
     SPDQLLDSLL PLYLQNQVLR ALQESAASEL ACRMTAMNNA SDNAKELAST LNLTYNKARQ
     AAITQEILEV VGGSVV
 
 
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