ATPG_SYNR3
ID ATPG_SYNR3 Reviewed; 315 AA.
AC A5GV71;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=SynRCC307_1877;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-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; CT978603; CAK28780.1; -; Genomic_DNA.
DR RefSeq; WP_011936293.1; NC_009482.1.
DR AlphaFoldDB; A5GV71; -.
DR SMR; A5GV71; -.
DR STRING; 316278.SynRCC307_1877; -.
DR EnsemblBacteria; CAK28780; CAK28780; SynRCC307_1877.
DR KEGG; syr:SynRCC307_1877; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_0_3; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR Proteomes; UP000001115; 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 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 Reference proteome; Thylakoid; Transport.
FT CHAIN 1..315
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000053365"
SQ SEQUENCE 315 AA; 34656 MW; 22DF836B1AC52A13 CRC64;
MANLKEIRDR IKSVKNTRKI TEAMRLVAAA KVRRAQDLVL RSRPFADRLA RVLESLQSRI
ALESADTPLL QARDPRHITL VAMTGDRGLC GGFNANIIKR TEQRFAELKA SGYEVALITV
GRKVDTYFQN RNYPITASFT GLDQLPTSTD ALQVSDAVQA EFLGGATDRV ELIYTKFINL
VSTKPVSQTL LPLDPQGIAS PDDEIFRFVT KEGELGVERS SASNQEDKLK SDLVFEQSPS
QLLDVLLPLY LQNQVLRSLQ ESAASELASR MTAMNNASDN AKALAKELTL DYNKARQAAI
TQEILEVVGG ASAMA
