ID A0A0T5NVR7_9RHOB Unreviewed; 512 AA.
AC A0A0T5NVR7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=XM53_07705 {ECO:0000313|EMBL:KRS13033.1};
OS Roseovarius atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS13033.1, ECO:0000313|Proteomes:UP000051295};
RN [1] {ECO:0000313|EMBL:KRS13033.1, ECO:0000313|Proteomes:UP000051295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R12B {ECO:0000313|EMBL:KRS13033.1,
RC ECO:0000313|Proteomes:UP000051295};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius sp.R12b.";
RL Submitted (APR-2015) 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:KRS13033.1}.
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DR EMBL; LAXJ01000007; KRS13033.1; -; Genomic_DNA.
DR RefSeq; WP_057791974.1; NZ_LAXJ01000007.1.
DR AlphaFoldDB; A0A0T5NVR7; -.
DR STRING; 1641875.XM53_07705; -.
DR PATRIC; fig|1641875.4.peg.3942; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000051295; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}; Cell membrane {ECO:0000256|HAMAP-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}; Hydrolase {ECO:0000313|EMBL:KRS13033.1};
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..91
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 149..374
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 381..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 372
FT /note="Required for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ SEQUENCE 512 AA; 55320 MW; 7FA8749AC474FABC CRC64;
MGIQAAEISA ILKDQIKNFG QEAEVAEVGR VLSVGDGIAR VHGLDNVQAG ELVEFPGNIM
GMALNLETDN VGVVIFGSDR DIKEGDTVKR TKSIVDVPIG DELLGRVVDG LGNPLDGKGP
IKASTRGVAD VKAPGIIPRK SVHEPMATGL KSVDAMIPIG RGQRELIIGD RQTGKTAVAL
DTMLNQKSYN DAAGDDEYKK LYCVYVAVGQ KRSTVAQLVK KLEEAGAMDY SIVVAATASD
PAPMQFLAPY SATAMAEHFR DNGRHALIVY DDLSKQAVAY RQMSLLLRRP PGREAYPGDV
FYLHSRLLER SAKLNEDNGS GSLTALPIIE TQGGDVSAFI PTNVISITDG QIFLETELFY
QGIRPAVNTG LSVSRVGSSA QTNAMKSVAG PVKLSLAQYR EMAAFAQFGS DLDAATQRLL
SRGERLTELM KQPQYSPLTN AEIVCIIYAG TNGYLDKIKV DQVGRFEDGL LNHMRTKRKD
VLDWITNEDP KIKGDAEDKL KSAIEEFAAD FG
//
