ID   ATPA_UREP2              Reviewed;         799 AA.
AC   B1AIC1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=ATP synthase subunit alpha;
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 sector subunit alpha;
DE   AltName: Full=F-ATPase subunit alpha;
GN   Name=atpA; OrderedLocusNames=UPA3_0138;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The alpha chain is a regulatory subunit (By
CC       similarity). {ECO:0000250}.
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   -!- 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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; CP000942; ACA32826.1; -; Genomic_DNA.
DR   RefSeq; WP_006689132.1; NC_010503.1.
DR   AlphaFoldDB; B1AIC1; -.
DR   SMR; B1AIC1; -.
DR   PRIDE; B1AIC1; -.
DR   EnsemblBacteria; ACA32826; ACA32826; UPA3_0138.
DR   GeneID; 29672716; -.
DR   KEGG; upa:UPA3_0138; -.
DR   HOGENOM; CLU_019180_0_0_14; -.
DR   OMA; EDENHEY; -.
DR   OrthoDB; 185156at2; -.
DR   Proteomes; UP000002162; 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   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); Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..799
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_0000339065"
FT   REGION          1..549
FT                   /note="ATP synthase alpha chain"
FT   REGION          550..799
FT                   /note="Unknown"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            363
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   799 AA;  89447 MW;  1A63E0F5C8982C8B CRC64;
     MTDNKNHSLI SDIKSQIKKF SEKALTLEVG NVISLGDGIV LVDGLDNVML NEIVRFENGV
     EGMALNLEED AVGVVLLGDY SNIKEGDRVY RTKRIVEVPV GDVMLGRVVD ALGKAVDNKG
     NIVANKFSVI EKIAPGVMDR KSVHQPLETG ILSIDAMFPI GKGQRELIIG DRQTGKTTIA
     IDAIINQKGR NVNCVYVAIG QKNSTIANVV RELEAHGAME YTTVVTANAS ELPALQYIAP
     FTGVTIAEEW MHQGKDVLIV YDDLSKHAIA YRTLSLLLRR PPGREAYPGD VFYLHSRLLE
     RACKLKDELG AGSITALPII ETQAGDISAY IPTNVISITD GQIFMMTSLF NAGQRPAIDA
     GQSVSRVGSA AQIKSVKQTG ASLKLELANY RELEAFSQFG SDLDDETKRI LKLGKAVMAV
     IKQAPNKPYN QTDEAIILFT VKEKLIPQVP VERIQDFKEY LLNYFKGTKL RADLEDKKAF
     DKENTPAFRC AIQKAINSFL NNSQDFKPCE EAEQTAFDKF FNENESIVVD GENDFNFINE
     EVSLKPTTET SEAVQIEEKV QDFVEPQEIL ETNKMEENHI FEEVEPEKII CEHHEFEIAE
     NQEKIEGQQV LEDTNHEYSI YETVEQSGEV DNDESKDDDL EVLVPVAEIE HDEAILDERE
     NRNWVFSDSA VSEVEKQTIM ISISSNEAEQ LFDNAKSVVF FKVTPKYPVE KVLVYVTSPV
     QKVVGEFDLL KIDVNSVNTS WNKYRSSSVI SSRKEYLEYF NSHKEAHALL ASKVYKYRKP
     KDLASFNMNK GPSGFTYLK