ID A0A433RNC0_9BACL Unreviewed; 504 AA.
AC A0A433RNC0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
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=ELR57_02185 {ECO:0000313|EMBL:RUS49169.1};
OS Cohnella sp. AR92.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=648716 {ECO:0000313|EMBL:RUS49169.1, ECO:0000313|Proteomes:UP000267180};
RN [1] {ECO:0000313|EMBL:RUS49169.1, ECO:0000313|Proteomes:UP000267180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR92 {ECO:0000313|EMBL:RUS49169.1,
RC ECO:0000313|Proteomes:UP000267180};
RX PubMed=29166641; DOI=10.1159/000480541;
RA Pisa J.H., Manfredi A.P., Perotti N.I., Romero H.G., Breccia J.D.,
RA Martinez M.A.;
RT "Agrowastes as Feedstock for the Production of Endo-?-Xylanase from
RT Cohnella sp. Strain AR92.";
RL J. Mol. Microbiol. Biotechnol. 27:277-288(2017).
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:RUS49169.1}.
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DR EMBL; RZJR01000001; RUS49169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433RNC0; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000267180; 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|HAMAP-Rule:MF_01346};
KW Hydrolase {ECO:0000313|EMBL:RUS49169.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000267180};
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 27..92
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 149..364
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 371..496
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
FT SITE 362
FT /note="Required for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ SEQUENCE 504 AA; 54471 MW; 27D946B185391595 CRC64;
MSIRPEEIST LIKQQIEQYQ SDIQVVDVGT VIQVSDGIAR VHGLENAMAG ELLEFADGTV
GMALNLEESN VGVVIMGPYT GIREGDQVKR TGRVMEVPVG EALLGRVVNA LGQPVDGEGP
IKTTKTRPVE SPAPGVMARK SVHEPMQTGI KAIDAMIPIG RGQRELIIGD RQTGKTAIAI
DTIVNQKGNG VICIYVAIGQ KQSTVRNVVE SLRRSGALEY TIVVTASASE PSPLLYVAPY
TGCAMGEEFM YNGKHVLIVY DDLSKQAAAY REMSLLLRRP PGREAFPGDV FYLHSRLLER
AAKLNDELGG GSMTALPFIE TQAGDVSAYI PTNVISITDG QIFLEADLFY SGQRPAVNVG
ISVSRVGGSA QTKAMKKVAG TLKTDLAQYR ELAAFAAFGS DLDKVTQSRL DRGVRTLEIL
KQGINVPMPF ERQVLSLYIV TRGHADSIPV QDVLRFEQEF LAYVDANKAE ILANIRDTKD
LTSDNEKALV EAIGAFKKGF ATTA
//
