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ATPA_ACEWD
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   03-AUG-2022, entry version 138.
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; 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=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   PRIDE; P50000; -.
DR   EnsemblBacteria; AFA47030; AFA47030; Awo_c02210.
DR   KEGG; awo:Awo_c02210; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_9; -.
DR   OMA; LQAPGVM; -.
DR   OrthoDB; 837522at2; -.
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; cd01132; F1_ATPase_alpha; 1.
DR   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 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.
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   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; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 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
 
 
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