ATPG_PROM3
ID ATPG_PROM3 Reviewed; 316 AA.
AC A2C6X6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=P9303_04841;
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303;
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; CP000554; ABM77236.1; -; Genomic_DNA.
DR AlphaFoldDB; A2C6X6; -.
DR SMR; A2C6X6; -.
DR STRING; 59922.P9303_04841; -.
DR EnsemblBacteria; ABM77236; ABM77236; P9303_04841.
DR KEGG; pmf:P9303_04841; -.
DR HOGENOM; CLU_050669_0_0_3; -.
DR OMA; MQITSAM; -.
DR BioCyc; PMAR59922:G1G80-446-MON; -.
DR Proteomes; UP000002274; 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_1000053284"
SQ SEQUENCE 316 AA; 34988 MW; FEB3DD5B66F62FF0 CRC64;
MANLKDIRDR IVSVKNTRKI TEAMRLVAAA KVRRAQEQVL RSRPFADRLA RVLENIQSRM
SFEMADAPLL KTSDLKTITL LAVTGDRGLC GGYNSNIIKR TEQRYAELNG QGYKVDLVLI
GRKAITYFSN RSSQYTIRAT FTGLEQVPTS DDAESITTEV LAEFLSQSTD RIEVIYTKFI
NLVSCNPVVQ TLLPLDPQGI AEADDEIFRL TTKDSRLTVE KGVGPANEQP PLPSDIIFEQ
SPEQLLNALL PLYLQNQMLR ALQESAASEL ASRMTAMNNA SDNAKALAKT LTLDYNKARQ
AAITQEILEV VGGSCS
