ATPG_ACEWD
ID ATPG_ACEWD Reviewed; 302 AA.
AC P50005; H6LG95;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ATP synthase gamma chain, sodium ion specific;
DE AltName: Full=F-ATPase gamma subunit, sodium ion specific;
DE AltName: Full=Na(+)-translocating ATPase gamma chain;
GN Name=atpG; Synonyms=uncG; OrderedLocusNames=Awo_c02220;
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=7748890; DOI=10.1016/0005-2728(95)00037-j;
RA Forster A., Daniel R., Mueller V.;
RT "The Na(+)-translocating ATPase of Acetobacterium woodii is a F1F0-type
RT enzyme as deduced from the primary structure of its beta, gamma and epsilon
RT subunits.";
RL Biochim. Biophys. Acta 1229:393-397(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-9.
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=8033902; DOI=10.1111/j.1432-1033.1994.tb18992.x;
RA Reidlinger J., Mueller V.;
RT "Purification of ATP synthase from Acetobacterium woodii and identification
RT as a Na(+)-translocating F1F0-type enzyme.";
RL Eur. J. Biochem. 223:275-283(1994).
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 -!- ACTIVITY REGULATION: Inhibited by nitrate.
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; U10505; AAA79907.1; -; Genomic_DNA.
DR EMBL; CP002987; AFA47031.1; -; Genomic_DNA.
DR PIR; I39747; I39747.
DR RefSeq; WP_014354634.1; NC_016894.1.
DR AlphaFoldDB; P50005; -.
DR SMR; P50005; -.
DR STRING; 931626.Awo_c02220; -.
DR TCDB; 3.A.2.1.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PRIDE; P50005; -.
DR EnsemblBacteria; AFA47031; AFA47031; Awo_c02220.
DR KEGG; awo:Awo_c02220; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_1_9; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR Proteomes; UP000007177; Chromosome.
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; 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 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8033902"
FT CHAIN 2..302
FT /note="ATP synthase gamma chain, sodium ion specific"
FT /id="PRO_0000073217"
FT CONFLICT 10
FT /note="R -> P (in Ref. 1; AAA79907)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> R (in Ref. 1; AAA79907)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="F -> L (in Ref. 1; AAA79907)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> P (in Ref. 1; AAA79907)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..302
FT /note="ALN -> D (in Ref. 1; AAA79907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 34016 MW; ADD79E74428C37C2 CRC64;
MAENVQDIKR RIKSVNSTMQ ITHAMELVAS AKLRKSRELA EGRRPYFEAM IESIGRIVEK
SGNARNIFMD QREVKKTAYI IITGDKGLAG GYNVNVAKLV EEHITDKENA VLFTVGSRGR
DHFRNREYHI QGEYLGISER PNFFNAKEVT AIVMEGFKNG EYDEVYIAYT KFVSTITQHA
QMMKLLPLSA EELITSGKVK TTEETKEEKS KMSDRELTIM TYEPEPEELL KYLIPNFVSS
TVYGSMIESA ASEQGARRTA MESATTNANE MIDGLTLQYN RVRQAAITQE ISEIVGGAEA
LN
