ATPG_SYNSC
ID ATPG_SYNSC Reviewed; 316 AA.
AC Q3AHK6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=Syncc9605_2187;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) 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; CP000110; ABB35926.1; -; Genomic_DNA.
DR RefSeq; WP_011365130.1; NC_007516.1.
DR AlphaFoldDB; Q3AHK6; -.
DR SMR; Q3AHK6; -.
DR STRING; 110662.Syncc9605_2187; -.
DR PRIDE; Q3AHK6; -.
DR EnsemblBacteria; ABB35926; ABB35926; Syncc9605_2187.
DR KEGG; syd:Syncc9605_2187; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_0_3; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
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 Thylakoid; Transport.
FT CHAIN 1..316
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000053368"
SQ SEQUENCE 316 AA; 34803 MW; B415D5FC3F657B7F CRC64;
MANLKEIRDR IKSVKNTRKI TEAMRLVAAA KVRRAQEQVL RSRPFADRLA RILENLQSRM
GFEDAASPLM QQRNVETITL VAVTGDRGLC GGYNANIIKR TEQRFAELKG KGFDVKLLLI
GTKAIGYFTR RDYPIQATFS GLEQVPTADE ANTISTDLLA EFLAESTDRV ELIFTKFINL
VSCKPVVQTL LPLDPQDIAD PEDEIFRLTT KDGLLTVEPG AGPANTEPKI PSDIVFEQTP
EQLLNALLPL YLQNQLLRSL QESAASELAS RMTAMNNASD NAKELAKTLT LDYNKARQAA
ITQEILEVAG GAAAVG
