ATPA_ORITI
ID ATPA_ORITI Reviewed; 512 AA.
AC B3CSS9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=OTT_0968;
OS Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=334380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ikeda;
RX PubMed=18508905; DOI=10.1093/dnares/dsn011;
RA Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M.,
RA Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K.,
RA Tamura A., Hattori M., Hayashi T.;
RT "The whole-genome sequencing of the obligate intracellular bacterium
RT Orientia tsutsugamushi revealed massive gene amplification during reductive
RT genome evolution.";
RL DNA Res. 15:185-199(2008).
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}.
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; AP008981; BAG40426.1; -; Genomic_DNA.
DR RefSeq; WP_012461551.1; NC_010793.1.
DR AlphaFoldDB; B3CSS9; -.
DR SMR; B3CSS9; -.
DR PRIDE; B3CSS9; -.
DR EnsemblBacteria; BAG40426; BAG40426; OTT_0968.
DR GeneID; 66653016; -.
DR KEGG; ott:OTT_0968; -.
DR HOGENOM; CLU_010091_2_1_5; -.
DR OMA; LQAPGVM; -.
DR OrthoDB; 837522at2; -.
DR Proteomes; UP000001033; 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 Translocase; Transport.
FT CHAIN 1..512
FT /note="ATP synthase subunit alpha"
FT /id="PRO_1000143417"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 370
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 512 AA; 56530 MW; 299F0FF9B55DD9B9 CRC64;
MQLKASEVYE ALKKQLEDFD ELSELSEVGY VISIGDGIAK VYGLSNAYSG EILQFSTGTK
GIVFSLKDNL IEAVVIGSDD QIKQGSQVKR TQTSLKVPTG KELLGRVVDA VGNPIDGKGE
FINPTYLDVE VKAPSVMCRD SVNEPMYTGI KAIDALIPIG KGQRELIIGD RQTGKTAIAI
DIILNQKRFH LSDQEREKVY CIYVAIGQKR STVAQLVKKL QETGAMAYTT VVLSSASDAA
SLQYLAPYTG CAIGEYFRDN GMHALVIYDD LSKHAIAYRQ ISLLLRRPPA REAYPGDVFY
LHSRLLERAA KLNKAKGEGS LTALPIVETQ NSDVSAYIPT NIISITDGQI FLESELFYKG
TKPALNVGIS VSRVGAAAQI KAMKDIAGTV KLELAQYHEM EAFSQFGADL DSSSMQLINR
GRRLSELLKQ SQYCPFSVEE QIIVLFAGIN GYLDKVAVSK VKEFESNMLE HFRIHNPDIM
NEIISTKKIT EIISSKLHQI LQEFVKSIEQ YS
