ID A0A3B9TZA5_9RHOB Unreviewed; 453 AA. AC A0A3B9TZA5; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 11-DEC-2019, entry version 6. DE SubName: Full=F0F1 ATP synthase subunit alpha {ECO:0000313|EMBL:HAG25369.1}; DE Flags: Fragment; GN ORFNames=DCK86_00905 {ECO:0000313|EMBL:HAG25369.1}; OS Rhodobacter sp. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1062 {ECO:0000313|EMBL:HAG25369.1, ECO:0000313|Proteomes:UP000258312}; RN [1] {ECO:0000313|EMBL:HAG25369.1, ECO:0000313|Proteomes:UP000258312} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA9917 {ECO:0000313|EMBL:HAG25369.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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:HAG25369.1}. 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; DMDJ01000024; HAG25369.1; -; Genomic_DNA. DR Proteomes; UP000258312; Unassembled WGS sequence. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR CDD; cd01132; F1_ATPase_alpha; 1. DR Gene3D; 1.20.150.20; -; 1. DR Gene3D; 2.40.30.20; -; 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; FT DOMAIN 1..32 FT /note="ATP-synt_ab_N" FT /evidence="ECO:0000259|Pfam:PF02874" FT DOMAIN 90..315 FT /note="ATP-synt_ab" FT /evidence="ECO:0000259|Pfam:PF00006" FT DOMAIN 322..448 FT /note="ATP-synt_ab_C" FT /evidence="ECO:0000259|Pfam:PF00306" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:HAG25369.1" SQ SEQUENCE 453 AA; 48933 MW; 3B994A77D1A285A4 CRC64; RGMALNLEVD NVGVVIFGDD RAIKEGDTVK RTKSIVDVPV GEGLLGRVVD GLGNPIDGKG PIVSSERRVA DVKAPGIIPR KSVHEPMATG LKSVDAMIPV GRGQRELIIG DRQTGKTAIA LDTILNQKSY NKAAGKDEGK KLYCIYVAIG QKRSTVAQLV RKLEETGALE YTIVVAATAS DPAPLQFLAP YAATSMAEYF RDNGRHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RSAKLNAENG SGSLTALPII ETQGGDVSAF IPTNVISITD GQIFLETELF YQGIRPAVNT GLSVSRVGSS AQTDAMKSVA GPVKLELAQY REMAAFAQFG SDLDASTQQL LNRGARLTEL MKQPQYAPLT NAEIVCVIFA GTKGYLDKIP VGDVGRFESG LLQYLRTTGK DVLEDITKND RKVKGDLEDK IKAALNAFAK DFA //