ID A0A1F5G239_9BACT Unreviewed; 347 AA.
AC A0A1F5G239;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=F0F1 ATP synthase subunit alpha {ECO:0000313|EMBL:OGD85895.1};
DE Flags: Fragment;
GN ORFNames=A2696_03495 {ECO:0000313|EMBL:OGD85895.1};
OS Candidatus Curtissbacteria bacterium RIFCSPHIGHO2_01_FULL_41_13.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797745 {ECO:0000313|EMBL:OGD85895.1, ECO:0000313|Proteomes:UP000177069};
RN [1] {ECO:0000313|EMBL:OGD85895.1, ECO:0000313|Proteomes:UP000177069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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:OGD85895.1}.
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DR EMBL; MFBA01000011; OGD85895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5G239; -.
DR Proteomes; UP000177069; Unassembled WGS sequence.
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-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_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; PF02874; ATP-synt_ab_N; 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-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 22..98
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 155..347
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT NON_TER 347
FT /evidence="ECO:0000313|EMBL:OGD85895.1"
SQ SEQUENCE 347 AA; 37225 MW; D267D64D27F8A735 CRC64;
MGILEEIEKQ IDKAKLTTTA KNVGKVAEIG DGVARVSGLS DVGASELVQF HPSGPEALRA
GGHNVTGLAL NLEEDSVGII VFGDWTKLKE GDTCQTTGKI LEIPVGDDLV GRVIDPLGKP
LDGKGKIVTK KFYPAEKIAP GVIYRRPVNT PLQTGLKAID SMIPIGRGQR ELIIGDRGLG
KTAICLDTII NQKDQKAICI YVAIGQKTSK IAQVVATLEK HKALNHTIVV AASASDSATL
QYIAPYAGCA IGEYFMDQGK DALVVYDDLS KHAWAYRQIS LLLKRPFGRE AYPGDIFYLH
SRLLERAARM DEKYGGGSLT ALPVIETQAG DVSAYIPTNV ISITDGQ
//
