ATPA_UREPA
ID ATPA_UREPA Reviewed; 799 AA.
AC Q9PR12;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=UU132;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30538.1; -; Genomic_DNA.
DR RefSeq; WP_006689132.1; NC_002162.1.
DR AlphaFoldDB; Q9PR12; -.
DR SMR; Q9PR12; -.
DR STRING; 273119.UU132; -.
DR EnsemblBacteria; AAF30538; AAF30538; UU132.
DR GeneID; 29672716; -.
DR KEGG; uur:UU132; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_019180_0_0_14; -.
DR OMA; EDENHEY; -.
DR Proteomes; UP000000423; 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; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..799
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000238393"
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