ID A0A4R5LE92_9BURK Unreviewed; 513 AA. AC A0A4R5LE92; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 24-JAN-2024, entry version 16. DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346}; DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01346}; DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346}; DE AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346}; GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346}; GN ORFNames=E1N52_13905 {ECO:0000313|EMBL:TDG07873.1}; OS Paraburkholderia guartelaensis. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=2546446 {ECO:0000313|EMBL:TDG07873.1, ECO:0000313|Proteomes:UP000295606}; RN [1] {ECO:0000313|EMBL:TDG07873.1, ECO:0000313|Proteomes:UP000295606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNPSo 3008 {ECO:0000313|EMBL:TDG07873.1, RC ECO:0000313|Proteomes:UP000295606}; RA Paulitsch F., Hungria M., Delamuta J.R.M., Ribeiro R.A., Dall'Agnol R., RA Silva J.S.B.; RT "Paraburkholderia sp. isolated from native Mimosa gymnas in Guartela State RT Park, Brazil."; RL Submitted (MAR-2019) 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:0000256|ARBA:ARBA00003784, ECO:0000256|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:0000256|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). CC {ECO:0000256|ARBA:ARBA00026013}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01346}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01346}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01346}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TDG07873.1}. 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; SMOD01000009; TDG07873.1; -; Genomic_DNA. DR RefSeq; WP_069264448.1; NZ_SMOD01000009.1. DR AlphaFoldDB; A0A4R5LE92; -. DR OrthoDB; 9803053at2; -. DR Proteomes; UP000295606; Unassembled WGS sequence. 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; cd18116; ATP-synt_F1_alpha_N; 1. DR CDD; cd01132; F1-ATPase_alpha_CD; 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 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 {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01346}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01346}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01346}. FT DOMAIN 25..92 FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF02874" FT DOMAIN 149..375 FT /note="ATPase F1/V1/A1 complex alpha/beta subunit FT nucleotide-binding" FT /evidence="ECO:0000259|Pfam:PF00006" FT DOMAIN 382..507 FT /note="ATP synthase alpha subunit C-terminal" FT /evidence="ECO:0000259|Pfam:PF00306" FT BINDING 169..176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346" FT SITE 373 FT /note="Required for activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346" SQ SEQUENCE 513 AA; 55870 MW; E768114329F17855 CRC64; MQLNPSEISE LIKSRIQGLE ASADVRNQGT VISVTDGIVR IHGLSDVMQG EMLEFPGNTF GLALNLERDS VGAVILGEYE HISEGDIVKT TGRILEVPVG PELIGRVVDP LGNPIDGKGP VNAKMTDAIE KIAPGVIWRE GVSQPVQTGL KSIDSMVPIG RGQRELIIGD RQCGKTAVAV DTIINQKGKD LICIYVAIGQ KASSIQNVLR KLEETGAIEY TIVVAASASE SAALQYLAPY AGCTMGEYFR DRGQDALIIY DDLTKQAWAY RQISLLLRRP PGREAYPGDV FYLHSRLLER AARVSADYVE KFTNGEVKGK TGSLTALPII ETQAGDVTAF VPTNVISITD GQIFLETDLF NAGIRPAINA GVSVSRVGGA AQTKVVKKLS GGIRTDLAQY RELAAFAQFA SDLDEATRKQ LERGRRVTEL LKQPQYQPLQ VWELAVALFS ANNGYLDDID VKDVLPFEKG LREYLKSKHA DLVARIEDKK DLSKDDENAL HAALKDFKKS GAY //