ID ATPA_ACEWD Reviewed; 502 AA.
AC P50000; H6LFT5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=ATP synthase subunit alpha, sodium ion specific;
DE EC=7.2.2.1;
DE AltName: Full=Na(+)-translocating ATPase subunit alpha;
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; Synonyms=uncA;
GN OrderedLocusNames=Awo_c02210;
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Bacillota; 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=10567365; DOI=10.1074/jbc.274.48.33999;
RA Rahlfs S., Aufurth S., Mueller V.;
RT "The Na+-F1FO-ATPase operon from Acetobacterium woodii: operon structure
RT and presence of multiple copies of atpE which encode proteolipids of 8- and
RT 18-kDa.";
RL J. Biol. Chem. 274:33999-34004(1999).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 452-501.
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).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a sodium ion
CC gradient across the membrane. The alpha chain is a regulatory subunit.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + 4 Na(+)(in) = ADP + H(+) + 4 Na(+)(out) +
CC phosphate; Xref=Rhea:RHEA:58156, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.1;
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:0000255|HAMAP-Rule:MF_01346};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; U10505; AAA79906.2; -; Genomic_DNA.
DR EMBL; CP002987; AFA47030.1; -; Genomic_DNA.
DR PIR; I39746; I39746.
DR RefSeq; WP_014354633.1; NC_016894.1.
DR AlphaFoldDB; P50000; -.
DR SMR; P50000; -.
DR STRING; 931626.Awo_c02210; -.
DR TCDB; 3.A.2.1.5; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR KEGG; awo:Awo_c02210; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_9; -.
DR OrthoDB; 9803053at2; -.
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:0046932; F:sodium-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046962; F:sodium-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Sodium; Sodium transport;
KW Translocase; Transport.
FT CHAIN 1..502
FT /note="ATP synthase subunit alpha, sodium ion specific"
FT /id="PRO_0000144311"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 360
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT CONFLICT 17
FT /note="E -> D (in Ref. 1; AAA79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..104
FT /note="VEVPVGEAMI -> LKFQLANHVF (in Ref. 1; AAA79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..180
FT /note="AI -> GF (in Ref. 1; AAA79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 235..236
FT /note="QY -> HN (in Ref. 1; AAA79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..264
FT /note="NEQQKDVLIIYDDL -> KGPTKRITVHQGRP (in Ref. 1;
FT AAA79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..278
FT /note="AVAYRAMSLIL -> GCLPSLVFDP (in Ref. 1; AAA79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> P (in Ref. 1; AAA79906)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="D -> G (in Ref. 1; AAA79906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 55019 MW; BDBAB11E4C8E1AB0 CRC64;
MNLRPEEISQ IIKNEIERYE DKLEVVDVGT VIQVGDGVAR VHGLENAMAG ELLAFPNEVY
GMVLNLEEDN VGCVLLGYDD DIVEGDIVRC TGRIVEVPVG EAMIGRVVNA LGFPVDGKGP
IVTDHRRPVE VKAAGVIERE SVNQPIQTGY KAIDSMIPIG RGQRELIIGD RQTGKTALAI
DTIINQKGED VICIYVAIGQ KDSTVAQIVG QLEENNAMDY TIIVSAGAAQ LAPLQYIAPY
SGVTMAEYFM NEQQKDVLII YDDLSKHAVA YRAMSLILRR PPGREAYPGD VFYLHSRLLE
RAAKLKAGGS ITALPIIETQ AGDVSAYIPT NVISITDGQI FLEAELFRSG IRPAVNPGIS
VSRVGGSAQI KSMKKVAGPL RIEYAQYREL ASFAQFGSDL DDETKAQLAK GERIVEILKQ
DQYDPMNVED QVLILYAATN GFLLDIEVKD IREFEKGLIK FAQKKYPEIM TKVKGKDGLS
DEVVAAFAEC IEAYKKVFSK SV
//
