ID   ATPA1_CHLL3             Reviewed;         511 AA.
AC   Q3B3Z9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=ATP synthase subunit alpha 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01346};
GN   Name=atpA1 {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=Plut_1070;
OS   Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS   luteolum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273 / BCRC 81028 / 2530;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) 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.
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 four main
CC       subunits: a(1), b(1), b'(1) and c(9-12) (By similarity). {ECO:0000250}.
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; CP000096; ABB23932.1; -; Genomic_DNA.
DR   RefSeq; WP_011357804.1; NC_007512.1.
DR   AlphaFoldDB; Q3B3Z9; -.
DR   SMR; Q3B3Z9; -.
DR   STRING; 319225.Plut_1070; -.
DR   EnsemblBacteria; ABB23932; ABB23932; Plut_1070.
DR   KEGG; plt:Plut_1070; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_10; -.
DR   OMA; VICIYCA; -.
DR   OrthoDB; 837522at2; -.
DR   Proteomes; UP000002709; 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   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; IPR017710; Alt_ATP_synth_F1_asu.
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; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
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   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03324; alt_F1F0_F1_al; 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..511
FT                   /note="ATP synthase subunit alpha 1"
FT                   /id="PRO_0000238315"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            367
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   511 AA;  55555 MW;  BD31C72CEAD22DC8 CRC64;
     MQEKTLTESI DAALSSIGEA SRTTQPEIEL RENGVVTTVL NGIALIRGLP GVGYEELVEM
     SGGVYGIAFN VDPDEVGVVL LGEYAKLQAG GRARRTGRVM DVPVGDGLLG RVVNPLGRPL
     DAEGEPRFSG RLPIERPSPG IMDRNAVSTP LQTGLKVVDA IVPIGRGQRE LILGDRQTGK
     TAIAVATILN QKGRNVICIY CAIGQRASAV AKVLAQLREH GAMAHTVAVV TEGNDPSGLQ
     YIAPYAATSI GEYFMEQGRD VLIVYDDLTN HARAYRELSL LLKRPPGREA FPGDIFYVHS
     RLLERSTHLR KELGGGSLTA LPIIETEAQN ISAYIPTNLI SITDGQIYLS PTLFELGNLP
     AVDIGKSVSR VGGKAQLAAY RSVTGRLKLA YAQFEELENF ARFGTRLDEA SRKAITHGER
     IRECLKQDEL DVLGVEEQIL ILLSLSEGQF DPLELSEVSG AMKRLSAAAR ELPRDLLERL
     HSDRPLSDED RRRLLQTAEA ALQKKRTAGR L