ID V5RWB2_9BACT Unreviewed; 511 AA.
AC V5RWB2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=RAAC3_TM7C00001G0684 {ECO:0000313|EMBL:AHB42527.1};
OS Candidatus Saccharibacteria bacterium RAAC3_TM7_1.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1394711 {ECO:0000313|EMBL:AHB42527.1, ECO:0000313|Proteomes:UP000018523};
RN [1] {ECO:0000313|EMBL:AHB42527.1, ECO:0000313|Proteomes:UP000018523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAAC3_TM7_1 {ECO:0000313|EMBL:AHB42527.1,
RC ECO:0000313|Proteomes:UP000018523};
RA Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA Castelle C.J., Thomas B.C., Banfield J.F.;
RT "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT four candidate phyla.";
RL Submitted (NOV-2013) 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|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}.
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DR EMBL; CP006915; AHB42527.1; -; Genomic_DNA.
DR AlphaFoldDB; V5RWB2; -.
DR STRING; 1394711.RAAC3_TM7C00001G0684; -.
DR KEGG; sbe:RAAC3_TM7C01G0684; -.
DR PATRIC; fig|1394711.4.peg.614; -.
DR HOGENOM; CLU_010091_2_1_0; -.
DR Proteomes; UP000018523; Chromosome.
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; 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; 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 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.
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|HAMAP-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}; Reference proteome {ECO:0000313|Proteomes:UP000018523};
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 28..93
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 153..370
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 377..485
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
FT SITE 368
FT /note="Required for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ SEQUENCE 511 AA; 54987 MW; FBA2E89494BD83BC CRC64;
MAELNVAELS KELQSAIAGL EGSEGLKDAG VVIRVGDGVA WVHGLKEAGY SEVLEIDTKK
GVVEAFALNL MEDEIGAVIL GDDSQVAAGD TVRLKGVVLE VPVGEELLGR VVDPLGRPLD
GGSAIKTKRT GRVEREAIGV MGRKHVHEPL MTGIMAIDAM FPIGRGQREL IIGDRQTGKT
AIVLDTMINQ SKQKSGVVNI YVAIGQKLSK VARIVERLKQ EGVMEQTIVV ATGPSDPASM
LYLAPYAATA MGEYFRDNKG HALMVYDDLS KHAVAYRQMS LLLRRPPGRE AFPGDVFYLH
SRLLERSAKL SDDLGAGSLT ALPIIETQAG DISAYIPTNV ISITDGQIFM ETDLFNQGIR
PAISAGLSVS RVGGDAQTKT VKSVSGHLKL GLSQFRELAS FAQFGSDLDE ATKAQIDRGQ
RLTELLKQSQ YQPMSVWEQT ASIYAVSEGT FDSVPVAKIK DAQSAMLTKL WTDHKSEMHE
LDKGDEKVGT DSPAAKLIVN VAKSVAKGFE D
//
