ATPA_VESOH
ID ATPA_VESOH Reviewed; 513 AA.
AC A5CVI8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=COSY_0947;
OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Vesicomyosocius.
OX NCBI_TaxID=412965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA;
RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA Kato C., Kitagawa M., Kato I., Maruyama T.;
RT "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT clam, Calyptogena okutanii.";
RL Curr. Biol. 17:881-886(2007).
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; AP009247; BAF62046.1; -; Genomic_DNA.
DR RefSeq; WP_011930315.1; NC_009465.1.
DR AlphaFoldDB; A5CVI8; -.
DR SMR; A5CVI8; -.
DR STRING; 412965.COSY_0947; -.
DR PRIDE; A5CVI8; -.
DR EnsemblBacteria; BAF62046; BAF62046; COSY_0947.
DR KEGG; vok:COSY_0947; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_6; -.
DR OMA; LQAPGVM; -.
DR OrthoDB; 837522at2; -.
DR Proteomes; UP000000247; 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 inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Translocase; Transport.
FT CHAIN 1..513
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000302714"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 513 AA; 55794 MW; 9AE5506126141914 CRC64;
MQLNAHEISD LIKKQIEGFD FTAEARTEGS VVSVSDGIVR IHGLGDVQFG EMIEFSNNTF
GMALNLEQDS VGAVILGDYL HILEGDIVKC TNRLVEVPVG EAMLGRVVNP LGKAIDGKGD
IDAQGVRPLE VMAPGVIDRK SVDQPIQTGI KAIDAMVPVG RGQRELIIGD RQTGKTAVAI
DAIINQRDSG IRCVYVAIGQ KDSSVATVVR KLEEYGALAN TIIVVAGAAV SPALQYIAPY
AGCAMAEYFR DRGEDVLIVY DDLTKQAWAY REVSLLLKRP PGREAYPGDV FYLHSRLLER
ASRVNADYVE KMTNGKVKGQ TGSLTALPII ETQGGDVSAF VPTNVISITD GQIFLETDLF
NAGIRPAINV GLSVSRVGGA AQTNIIKKLG GGIRLDLAQY RELVAFAQFS SDLDVETKAQ
IDRGQRVTEL MKQNQYSPLS IAEMATLLFS ANSGLLDDIE VNKIVDFEVS LIAYMKVNQV
SLMNRINEIG NYNDKISNEL QVAIDDFKTN YTW
