ID ATPA1_PSYIN Reviewed; 519 AA. AC A1SS62; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 02-SEP-2026, entry version 118. 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=Ping_0470; OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17664 / CCUG 51855 / 37; RX PubMed=18460197; DOI=10.1186/1471-2164-9-210; RA Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J., RA Land M.L., Thompson L.S.; RT "Genomics of an extreme psychrophile, Psychromonas ingrahamii."; RL BMC Genomics 9:210-210(2008). 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; CP000510; ABM02327.1; -; Genomic_DNA. DR RefSeq; WP_011768886.1; NC_008709.1. DR AlphaFoldDB; A1SS62; -. DR SMR; A1SS62; -. DR STRING; 357804.Ping_0470; -. DR KEGG; pin:Ping_0470; -. DR eggNOG; COG0056; Bacteria. DR HOGENOM; CLU_010091_2_1_6; -. DR OrthoDB; 9803053at2; -. DR Proteomes; UP000000639; 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; 3.40.50.300:FF:000002; ATP synthase subunit alpha; 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; 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; 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; TIGR03324; alt_F1F0_F1_al; 1. 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 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..519 FT /note="ATP synthase subunit alpha 1" FT /id="PRO_0000339048" FT BINDING 172..179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346" FT SITE 365 FT /note="Required for activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346" SQ SEQUENCE 519 AA; 56659 MW; 019CD2CBBB022332 CRC64; MTDLQQVVAH SFAALAASRT TFRAQLKARE IGIISSVSFG VAQVSGLANV ASEEVLKFSG DIYGIAFNVD QDSIGVVLLG DYWQLQSGDE VERTGRVMDV AVGLGLLGRV IDPLGRPLDD KGPIESSERL PVERPAAPIM DRAPVTVPLQ TGLKVIDALI PIGRGQRELI LGDRQTGKTT IAIDTILNQH DQNVLCVYCA IGQRASAVAK TIAILKAKGA LDYTLVMVSE GNAPPGFAYI APYAATSIAE YFMEKGRDVL IVYDDLTQHA RAYRELSLLL RRPPGREAFP GDIFYIHSRL LERATCLKQR HKGGSLTALP IIETEAQNIS AYIPTNLISI TDGQIYLSPT LFELGILPAV DVGRSVSRVG GKAQRPMYRA VAANLKLTYA QFEELETFAR FGARLDQNSQ DIITNGRRIR ASLKQPQSSP MTVLEQITVL IALTEKLFDT VPLLKMREAE QALCLATTEL PEDFLSRFNS AKILSDDDRN RIIDIARITL APFQSPPDED NGITSTPSN //