ID A0A7Z0C2T5_9ACTN Unreviewed; 544 AA.
AC A0A7Z0C2T5;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, 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=BKA05_001137 {ECO:0000313|EMBL:NYI09622.1};
OS Nocardioides marinus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=374514 {ECO:0000313|EMBL:NYI09622.1, ECO:0000313|Proteomes:UP000537326};
RN [1] {ECO:0000313|EMBL:NYI09622.1, ECO:0000313|Proteomes:UP000537326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18248 {ECO:0000313|EMBL:NYI09622.1,
RC ECO:0000313|Proteomes:UP000537326};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUL-2020) 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 + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out);
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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:NYI09622.1}.
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DR EMBL; JACBZI010000001; NYI09622.1; -; Genomic_DNA.
DR RefSeq; WP_179530570.1; NZ_BAAAPP010000012.1.
DR AlphaFoldDB; A0A7Z0C2T5; -.
DR Proteomes; UP000537326; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProtKB-KW.
DR GO; GO:0043531; F:ADP binding; IEA:TreeGrafter.
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 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 FunFam; 1.20.150.20:FF:000001; ATP synthase subunit alpha; 1.
DR FunFam; 3.40.50.300:FF:000002; ATP synthase subunit alpha; 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 NCBIfam; NF009884; PRK13343.1; 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.
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};
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|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:UP000537326};
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 30..96
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 153..376
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 384..497
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
FT REGION 518..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 544 AA; 58901 MW; 6BF9600598DC6B0B CRC64;
MTELSIRPDE IRDALQKYVA DYQPDAATRE EVGTVAQAAD GIARVSGLPS AMANELLEFE
DGTLGLALNL DTREIGVVIL GDFDKIEEGQ TVRRTGEILS VPVGDGFMGR VVDPLGKPID
GLGEIASDTR RALELQAPNV VQRKSVHEPL ATGIKAIDSM TPIGRGQRQL IIGDRATGKT
TIAIDTIINQ KQNWESGDPT KQVRCIYVAI GQKGSTIASV RGALEEAGAL EYTTIVAAPA
SDSAGFKYLA PYTGSAIGQQ WMYDGKHVLI VFDDLTKQAE AYRAVSLLLR RPPGREAYPG
DVFYLHSRLL ERCAKLSDEL GAGSMTGLPI IETKANDVSA FIPTNVISIT DGQIFLQSDL
FAANQRPAID VGVSVSRVGG AAMTKAMKAV TGSLKVDLAQ FRAMEAFAMF ASDLDAASRQ
QLDRGQRLMA LLKQPAYSPY ALEDMTVSLW LGTTGRLDKV PVQDVLRFEQ EFIDFVKRSH
EGILAAIRET QKFEDEDGLA AAYDAFLTQF ETSEGGAIKA GHEESEALED DELGQEQIVK
QKRG
//
