ATPA_BUCAP
ID ATPA_BUCAP Reviewed; 510 AA.
AC O51874;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
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=BUsg_006;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9216881; DOI=10.1007/s002849900217;
RA Clark M.A., Baumann P.;
RT "The (F1F0) ATP synthase of Buchnera aphidicola (endosymbiont of aphids):
RT genetic analysis of the putative ATP operon.";
RL Curr. Microbiol. 35:84-89(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9516544; DOI=10.1007/pl00006760;
RA Clark M.A., Baumann L., Baumann P.;
RT "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT gidA, and rho.";
RL Curr. Microbiol. 36:158-163(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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 -!- 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 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; AF008210; AAC38112.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67578.1; -; Genomic_DNA.
DR RefSeq; WP_011053544.1; NC_004061.1.
DR AlphaFoldDB; O51874; -.
DR SMR; O51874; -.
DR STRING; 198804.BUsg_006; -.
DR PRIDE; O51874; -.
DR EnsemblBacteria; AAM67578; AAM67578; BUsg_006.
DR KEGG; bas:BUsg_006; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_6; -.
DR OMA; MEVFTQF; -.
DR OrthoDB; 837522at2; -.
DR Proteomes; UP000000416; 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..510
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144321"
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 CONFLICT 269
FT /note="A -> R (in Ref. 1; no nucleotide entry and 2;
FT AAC38112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 56391 MW; EE2884411AFB5E3A CRC64;
MQLNSTEISQ LIKERIAQFE VFNQSYNEGT IISVNDGIIK IYGLSDVMLG EMILLPDNEY
AIALNIERDT IGAVVMGPYI HITEGTKVRC TGKILEVPVG VALLGRIVNA LGFPIDGKGS
IEHDIYLPVE ADAPGVIERE SINEPIQTGY KAIDAMVPIG RGQRELIIGD RQTGKTALAI
DTIINQKKIN LPCVYVAIGQ KLSTIINVVK KLDEHDALLN TIVVVASASE AASLQYLAPY
SGCAMGEYFR DRGKDALIVY DDLSKHAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER
ASRVSKEHVK NVTKGKITGK TGSLTALPII ETQSGDVSAF VPTNVISITD GQIFLESNLF
NSGIRPAVNA GISVSRVGSA AQTKIIKKLS SGIRTALAQY HELAAFSQFA SDLDQTTRKQ
LIYGQKITEL LKQKQYRPMS ISEQGLMFFI AENNFLDDIS VENIIQFEKE ILTYAYNYHL
DLMEEINKDG NFNDIIKKKF IELINNFKNS
