ID ATPA1_GLUOX Reviewed; 511 AA. AC Q5FRC7; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 04-NOV-2026, entry version 124. 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}; GN OrderedLocusNames=GOX1311; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Acetobacterales; Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H; RX PubMed=15665824; DOI=10.1038/nbt1062; RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., RA Ehrenreich A., Gottschalk G., Deppenmeier U.; RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). 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 + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000009; AAW61069.1; -; Genomic_DNA. DR RefSeq; WP_011252861.1; NC_006677.1. DR AlphaFoldDB; Q5FRC7; -. DR SMR; Q5FRC7; -. DR STRING; 290633.GOX1311; -. DR KEGG; gox:GOX1311; -. DR eggNOG; COG0056; Bacteria. DR HOGENOM; CLU_010091_2_1_5; -. DR OMA; AAFKQGW; -. DR Proteomes; UP000006375; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:InterPro. DR GO; GO:0043531; F:ADP binding; IEA:TreeGrafter. 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 CDD; cd18113; ATP-synt_F1_alpha_C; 1. DR CDD; cd18116; ATP-synt_F1_alpha_N; 1. DR CDD; cd01132; F1-ATPase_alpha_CD; 1. DR FunFam; 1.20.150.20:FF:000001; ATP synthase subunit alpha; 1. DR FunFam; 2.40.30.20:FF:000001; ATP synthase subunit alpha; 1. DR FunFam; 3.40.50.300:FF:002432; ATP synthase subunit alpha, mitochondrial; 1. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_nt-bd_dom. 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 NCBIfam; TIGR00962; atpA; 1. DR NCBIfam; NF009884; PRK13343.1; 1. DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Reference proteome; Translocase; Transport. FT CHAIN 1..511 FT /note="ATP synthase subunit alpha 1" FT /id="PRO_0000238258" FT BINDING 170..177 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346" FT SITE 371 FT /note="Required for activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346" SQ SEQUENCE 511 AA; 54952 MW; ACBC5BEE20FD3F8F CRC64; MDIRPAEISD ILKQQIASFD QVETVSETGT VLSIGDGIAR VYGLTNVMAG EMVEFEGTGL KGMALNLEAD NVGVVLFGDG DSIREGDTVL RTKSVVEVPV GKGLLGRVVD GLGNPIDGRG PLTDVEYRRA EVKAPGIMPR QSVSEPMQTG IKAIDALVPI GRGQRELIIG DRQTGKTAIL IDTIVAQKPV NAEGDPKKSL YCIYVAVGQK RSTVANLVRT LIEHGAMEYS IVVAATASDA APMQYLAPYT ACAMGEYFRD NGMHALVCYD DLSKQAVAYR QMSLLLRRPP AREAFPGDVF YLHSRLLERA AKMSDANGGG SLTALPVIET QAGDTAAYIP TNVISITDGQ IFLETDLFYR GIRPAVNVGG SVSRVGSAAQ IKAMKQVAGK IKLELAQYRE MAAFSQFASD LDAATRKQLD RGARLVELLK QPETSPLPVE EQVVVLYAGT RGYVDPIAVD KVVAYEAALL SELRGAGSDI LTAIRNDRQI KPETEGKLKE LLEAFGKRFS A //