ID A0A5J5FLV8_9GAMM Unreviewed; 514 AA. AC A0A5J5FLV8; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 07-OCT-2020, entry version 5. 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=F3089_07160 {ECO:0000313|EMBL:KAA8982896.1}; OS Halospina sp. K52047b. OC Bacteria; Proteobacteria; Gammaproteobacteria; Halospina. OX NCBI_TaxID=2614160 {ECO:0000313|EMBL:KAA8982896.1, ECO:0000313|Proteomes:UP000325621}; RN [1] {ECO:0000313|EMBL:KAA8982896.1, ECO:0000313|Proteomes:UP000325621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K52047b {ECO:0000313|EMBL:KAA8982896.1, RC ECO:0000313|Proteomes:UP000325621}; RA Bowman J.P.; RT "Genomes of a novel Halospina species."; RL Submitted (SEP-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 -!- 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:KAA8982896.1}. 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; VYJH01000004; KAA8982896.1; -; Genomic_DNA. DR Proteomes; UP000325621; 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; 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; 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 PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00962; atpA; 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 29..93 FT /note="ATP-synt_ab_N" FT /evidence="ECO:0000259|Pfam:PF02874" FT DOMAIN 150..376 FT /note="ATP-synt_ab" FT /evidence="ECO:0000259|Pfam:PF00006" FT DOMAIN 383..508 FT /note="ATP-synt_ab_C" FT /evidence="ECO:0000259|Pfam:PF00306" FT NP_BIND 170..177 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346" FT SITE 374 FT /note="Required for activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346" SQ SEQUENCE 514 AA; 55833 MW; 35ADBFD0F40CE50F CRC64; MQQLNPSEIS EIIKKRIEKL DVSSEARNEG TIVSVSDGIV RIHGLADVMY GEMVEFQNGN YGMALNLERD SVGAVVLGED EGLAEGQKVK CTGRILEVPV GRELLGRVVD ALGNPIDGKG DAGTTETTPI EKVAPGVIAR EEVNEPVQTG LKPIDTMVPV GRGQRELIIG DRQIGKTAVA VDTIINQKNS GIKCIYVAIG QKQSTIANVV RKLEEHGAMD NTIVVAAGAA DPASMQFLAP YAGTSMGEFF RDRGEDALII YDDLTKQAWA YRQISLLLRR PPGREAYPGD VFYLHSRLLE RASKVNPEYV EKATNGEVTG KTGSLTALPI IETQAGDVSA FVPTNVISIT DGQIFLETDL FNSGIRPAMN AGISVSRVGG SAQTKIMKKL GGGIRLALAQ YRELQAFAQF ASDLDEQTRK QLEHGARVTE LMKQEQYSPM SVGEMATVLF AANEGYLEDV DAKKIVDFEK ALMDYMRTEQ SELLAKINDS GELNDEVESG LKSALDKFKS TQSW //