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Database: UniProt
Entry: A0A1F6CGA2_9BACT
LinkDB: A0A1F6CGA2_9BACT
Original site: A0A1F6CGA2_9BACT 
ID   A0A1F6CGA2_9BACT        Unreviewed;       470 AA.
AC   A0A1F6CGA2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=ATPase F1/V1/A1 complex alpha/beta subunit nucleotide-binding domain-containing protein {ECO:0000259|Pfam:PF00006};
GN   ORFNames=A2678_01390 {ECO:0000313|EMBL:OGG48219.1};
OS   Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_53_31.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1798481 {ECO:0000313|EMBL:OGG48219.1, ECO:0000313|Proteomes:UP000178815};
RN   [1] {ECO:0000313|EMBL:OGG48219.1, ECO:0000313|Proteomes:UP000178815}
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:OGG48219.1}.
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DR   EMBL; MFKU01000016; OGG48219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6CGA2; -.
DR   STRING; 1798481.A2678_01390; -.
DR   Proteomes; UP000178815; 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:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 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};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          136..349
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   470 AA;  52049 MW;  C19052A37059FFCC CRC64;
     MEKITKPFVG SVRAVRGQVV VVHCESDYRP ALRELLTAED IPEIRMEVHS YYGRDLLHCL
     LLSSKEDLFR NMRIIALETT LSIPVGKGVL GRAINLYGQP LDGGKTLEYT DARSIYGTPH
     QTTLKVNQEH SLLETGIKII DFFAPMVEGG RLGIIGGAGV GKTAVMTEII HNLNQTHPGV
     TLFAGIGERI REGYELWDSL QTTGALAKTA LILAHINENA AVRFRVGAAA VTLAEYFRDE
     EKIDVLFFAD NIFRFVQAGN ELSTLLEEIP SEFGYQSTLQ SEIALFENRL VSTEDNSISS
     IQTVYVPADE LVDPAVAAAL PYFEATLVLS REMHQEGRFP AIDFLKSKSS VLDTLRASAD
     NPHFRVLTAA IEILNQYERL VRIVSIIGED ELSAQDRLIF DRASKLRNYM TQELFTLENQ
     TGKPGAYVKR TESIADVEAI LAGKFDSVPA DNFMYIGTTK DLEKSDSGPV
//
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