ATPA_THEMA
ID ATPA_THEMA Reviewed; 503 AA.
AC Q9X1U7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
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=TM_1612;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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}.
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DR EMBL; AE000512; AAD36679.1; -; Genomic_DNA.
DR PIR; F72231; F72231.
DR RefSeq; NP_229412.1; NC_000853.1.
DR RefSeq; WP_004082064.1; NZ_CP011107.1.
DR PDB; 2R9V; X-ray; 2.10 A; A=2-503.
DR PDBsum; 2R9V; -.
DR AlphaFoldDB; Q9X1U7; -.
DR SMR; Q9X1U7; -.
DR STRING; 243274.THEMA_06190; -.
DR DNASU; 897935; -.
DR EnsemblBacteria; AAD36679; AAD36679; TM_1612.
DR KEGG; tma:TM1612; -.
DR eggNOG; COG0056; Bacteria.
DR InParanoid; Q9X1U7; -.
DR OMA; LQAPGVM; -.
DR OrthoDB; 837522at2; -.
DR EvolutionaryTrace; Q9X1U7; -.
DR Proteomes; UP000008183; 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); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; Cell inner membrane;
KW Cell membrane; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..503
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000238387"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 363
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2R9V"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:2R9V"
FT TURN 186..191
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 233..251
FT /evidence="ECO:0007829|PDB:2R9V"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2R9V"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:2R9V"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:2R9V"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:2R9V"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 374..394
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 405..420
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:2R9V"
FT TURN 443..448
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 454..468
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:2R9V"
FT HELIX 484..500
FT /evidence="ECO:0007829|PDB:2R9V"
SQ SEQUENCE 503 AA; 56062 MW; 886C9736F16BF149 CRC64;
MRINPGEITK VLEEKIKSFE EKIDLEDTGK VIQVGDGIAR AYGLNKVMVS ELVEFVETGV
KGVAFNLEED NVGIIILGEY KDIKEGHTVR RLKRIIEVPV GEELLGRVVN PLGEPLDGKG
PINAKNFRPI EIKAPGVIYR KPVDTPLQTG IKAIDSMIPI GRGQRELIIG DRQTGKTAIA
IDTIINQKGQ GVYCIYVAIG QKKSAIARII DKLRQYGAME YTTVVVASAS DPASLQYIAP
YAGCAMGEYF AYSGRDALVV YDDLSKHAVA YRQLSLLMRR PPGREAYPGD IFYLHSRLLE
RAVRLNDKLG GGSLTALPIV ETQANDISAY IPTNVISITD GQIYLEPGLF YAGQRPAINV
GLSVSRVGGS AQIKAMKQVA GMLRIDLAQY RELETFAQFA TELDPATRAQ IIRGQRLMEL
LKQEQYSPMP VEEQVVVLFA GVRGYLDDLP VEEVRRFEKE FLRFMHEKHQ DILDDIKTKK
ELTSETEEKL KKAIEEFKTT FRV
