ATPG_MOOTA
ID ATPG_MOOTA Reviewed; 282 AA.
AC O05432; Q2RFX8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
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}; OrderedLocusNames=Moth_2379;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND OPERON STRUCTURE.
RX PubMed=9171425; DOI=10.1128/jb.179.11.3746-3755.1997;
RA Das A., Ljungdahl L.G.;
RT "Composition and primary structure of the F1F0 ATP synthase from the
RT obligately anaerobic bacterium Clostridium thermoaceticum.";
RL J. Bacteriol. 179:3746-3755(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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.
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 (By similarity). In this bacterium the a and b
CC subunits are transcribed but do not seem to be translated, thus the ATP
CC synthase consists of the alpha, beta, gamma, delta, epsilon and c
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00815,
CC ECO:0000269|PubMed:9171425}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00815}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U64318; AAB51465.1; -; Genomic_DNA.
DR EMBL; CP000232; ABC20661.1; -; Genomic_DNA.
DR RefSeq; WP_011393856.1; NC_007644.1.
DR RefSeq; YP_431204.1; NC_007644.1.
DR AlphaFoldDB; O05432; -.
DR SMR; O05432; -.
DR STRING; 264732.Moth_2379; -.
DR EnsemblBacteria; ABC20661; ABC20661; Moth_2379.
DR KEGG; mta:Moth_2379; -.
DR PATRIC; fig|264732.11.peg.2592; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_1_9; -.
DR OMA; MQITSAM; -.
DR GO; GO:0005886; C:plasma 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 GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; 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; 2.
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 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Transport.
FT CHAIN 1..282
FT /note="ATP synthase gamma chain"
FT /id="PRO_0000073314"
FT CONFLICT 42
FT /note="A -> G (in Ref. 1; AAB51465)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="Y -> N (in Ref. 1; AAB51465)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="A -> P (in Ref. 1; AAB51465)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> G (in Ref. 1; AAB51465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31653 MW; 5FEAA34C380E231D CRC64;
MAHMRDLKRR IRSVQSTQHI TRAMKMVAAA KLRKAQAQVT AARPYAAKLE EVVGRLMAAV
DPETQPLAAT REVKKAGYVL ITADRGLAGG YNANLIRLTE ERLREEGRPA ALVAVGRKGR
DFFRRRPVEI VKSFTDIGDN PELIQARELA RQLVTMYLEG TLDEVNLIYT RFYSAIRQVP
MVERLLPIAT PREKKDTGDY IYEPSPEAVL RVLLPRYCEI KVYRALLEAK ASEHGARMTA
MDNATKNAAE MIDKFTLSFN RARQAAITNE IVEIVAGADA LK
