ATPG_SYNS3
ID ATPG_SYNS3 Reviewed; 317 AA.
AC Q0I7R3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=sync_2312;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI46069.1; -; Genomic_DNA.
DR RefSeq; WP_011620221.1; NC_008319.1.
DR AlphaFoldDB; Q0I7R3; -.
DR SMR; Q0I7R3; -.
DR STRING; 64471.sync_2312; -.
DR EnsemblBacteria; ABI46069; ABI46069; sync_2312.
DR KEGG; syg:sync_2312; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_0_3; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR Proteomes; UP000001961; 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 Reference proteome; Thylakoid; Transport.
FT CHAIN 1..317
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000053366"
SQ SEQUENCE 317 AA; 34985 MW; 867D788F46A07E5B CRC64;
MANLKEIRDR IKSVKNTRKI TEAMRLVAAA KVRRAQEQVL RSRPFADRLA RLLENLQARM
RFEDADAPLL EQRAVQTITL MAVTGDRGLC GGYNSNIIKR TEKRFAELQR QGYKVALVLI
GRKAISYFTN RNYPIQATFT GLEQVPTADE AGSIASEIFA EFLSETSDRV EIIFTKFINL
VSCKPVVQTL LPLDPQGIAE ADDEIFRLTT KEGRLSVEAG SAPENSQPAL PSDIVFEQSP
DQLLNALLPL YLQNQLLRSL QESAASELAS RMTAMNNASD NAKELAKTLT LDYNKARQAA
ITQEILEVVG GSAAAGA