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ATPA_DICNV
ID   ATPA_DICNV              Reviewed;         513 AA.
AC   A5EXJ7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=DNO_1144;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The alpha chain is a regulatory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01346};
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(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       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; CP000513; ABQ14078.1; -; Genomic_DNA.
DR   RefSeq; WP_012031448.1; NC_009446.1.
DR   AlphaFoldDB; A5EXJ7; -.
DR   SMR; A5EXJ7; -.
DR   STRING; 246195.DNO_1144; -.
DR   PRIDE; A5EXJ7; -.
DR   EnsemblBacteria; ABQ14078; ABQ14078; DNO_1144.
DR   KEGG; dno:DNO_1144; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_6; -.
DR   OMA; LQAPGVM; -.
DR   OrthoDB; 837522at2; -.
DR   Proteomes; UP000000248; 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:0046961; F:proton-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 inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..513
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_0000339030"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            373
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   513 AA;  55295 MW;  5122BA6863589D01 CRC64;
     MQLNASEISS FIKDKIADYD NKVENKAEGT IVNVSDGIVQ IQGLSQAMLG EMIELPNGNF
     ALAMNLERDS VGAVVLGAYE HLREGDKVHC TGRILEVPVG RGLLGRVVDA LGNPIDGKGK
     IDAEGSSPVE KIAPGVIERQ SVDQPLQTGL KAIDSMVPLG RGQRELIIGD RQTGKTAIAI
     DAIINQKNTG VICIYVAIGQ KASSIASVVR KLEEADALKH TIVVAASAST SAAMQYIAPY
     SGCAMGEFFR DRGEDALIIY DDLTKQAWAY RQVSLLLRRP PGREAYPGDV FYLHSRLLER
     AARINAKEVE RLTAGKVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLETDLF
     NSGIRPAINA GLSVSRVGGA AQTQIIKKLG GGIRLALAQY RELAAFAQFA SDLDEATRKQ
     LEHGQRVTEL MKQKQYAPLS VAEMAISLFA ADKGYLDTVA VEDIMAYETA LLSFMRENHA
     DLMNTINTTG KYDEAVQTGL KEALDAFVEK RSL
 
 
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