ID A0A143LSQ6_LEPBO Unreviewed; 503 AA. AC A0A143LSQ6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-SEP-2016, entry version 3. DE RecName: Full=ATP synthase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346}; DE EC=3.6.3.14 {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=LBHA_10265 {ECO:0000313|EMBL:AMX68433.1}, LBHB_09425 GN {ECO:0000313|EMBL:AMX71484.1}; OS Leptospira borgpetersenii serovar Hardjo. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=328971 {ECO:0000313|EMBL:AMX71484.1}; RN [1] {ECO:0000313|EMBL:AMX71484.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVSL S 1343 {ECO:0000313|EMBL:AMX68433.1}, and NVSL S 818 RC {ECO:0000313|EMBL:AMX71484.1}; RA Llanes A., Restrepo C., Rajeev S.; RT "Genomic differences between Leptospira borgpetersenii serovar Hardjo RT laboratory strains and field isolates."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. {ECO:0000256|HAMAP-Rule:MF_01346}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000256|HAMAP-Rule:MF_01346}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01346}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|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; CP015050; AMX68433.1; -; Genomic_DNA. DR EMBL; CP015052; AMX71484.1; -; Genomic_DNA. DR RefSeq; WP_011670484.1; NZ_CP015052.1. DR GeneID; 4408290; -. 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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR CDD; cd01132; F1_ATPase_alpha; 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; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR023366; ATPase_asu-like. DR InterPro; IPR005294; ATPase_F1-cplx_asu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR033732; F1_ATPase_alpha. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR15184:SF3; PTHR15184:SF3; 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; SSF47917; 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 {ECO:0000256|HAMAP-Rule:MF_01346}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01346}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01346}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01346}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01346}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01346}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01346}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01346}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01346}. FT DOMAIN 26 91 ATP-synt_ab_N. {ECO:0000259|Pfam: FT PF02874}. FT DOMAIN 149 365 ATP-synt_ab. {ECO:0000259|Pfam:PF00006}. FT DOMAIN 372 487 ATP-synt_ab_C. {ECO:0000259|Pfam: FT PF00306}. FT NP_BIND 169 176 ATP. {ECO:0000256|HAMAP-Rule:MF_01346}. FT SITE 363 363 Required for activity. FT {ECO:0000256|HAMAP-Rule:MF_01346}. SQ SEQUENCE 503 AA; 54937 MW; C7413A98F8828EEC CRC64; MKIKTDEITS VLKQEILNYK KDLGVDEVGT VLEIGDGIAR VYGLKNVMSG EMVEFQNGIF GQAFNLEDNS VGVVVYGDYL AIQEGFTVKR TSRILEVPVG PELLGRVVNP LGEPLDGKGP INAKLTRPVE SPAPGIAMRQ PVGEPMQTGI KAIDAMIPIG RGQRELIIGD RGTGKTSIAL DTIINQKGTG VICVYVAIGQ KASTVASTVE MLRNKGALEY TIVVSATAAE PAPLQYIAPY SGCSMAEYFM YNEKKATLVV YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKLDDKYG AGSLTALPII ETQEGEVSAY IPTNVISITD GQIYLQSNLF ASGNRPAVDV GISVSRVGSA AQIKAMKQVA GKMKLELAQF RDLEAFAQLG TELDPATQAQ LDRGNRIVQM LKQPVSSPFP VEEQVVEIFA VTRGFMDKIP VPKVQQYGKF LLTRIKEQHS EVLEAIRKEK KISDEEKLGE VLSAIAEEFL RKH //