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Database: UniProt
Entry: A0A1F6IBZ0_9BACT
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ID   A0A1F6IBZ0_9BACT        Unreviewed;       477 AA.
AC   A0A1F6IBZ0;
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=A3D74_04000 {ECO:0000313|EMBL:OGH20057.1};
OS   Candidatus Levybacteria bacterium RIFCSPHIGHO2_02_FULL_37_13.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1798602 {ECO:0000313|EMBL:OGH20057.1, ECO:0000313|Proteomes:UP000177483};
RN   [1] {ECO:0000313|EMBL:OGH20057.1, ECO:0000313|Proteomes:UP000177483}
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:OGH20057.1}.
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DR   EMBL; MFNZ01000026; OGH20057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6IBZ0; -.
DR   STRING; 1798602.A3D74_04000; -.
DR   Proteomes; UP000177483; 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; 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.
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          130..363
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   477 AA;  52138 MW;  4EEDB3FB0246F488 CRC64;
     MDTTYGKIIG IQGHIIEVEF TQNQPKLHDI LVLEKDPSTK MEVFASKGRS TFYCISLSQM
     QKISRGMNVL STKKPILVPV GNGTLGRVID VFGNPLDELG EIKKDAELPI YKDSPSIKNI
     TYHQDLLETG IKVIDLFSPI VKGGKIGIFG GAGVGKTLLI TEIIHNVVGN PASQPASLSL
     GGKLQRSENS KESVSVFAGV GERIREGHEL YETLKDRGVL PFVALVLGTM GENPSVRFLT
     SFSAITIAEY FRDVLKKDVL FFIDNIFRFA QAGNELSVLM NTIPSEDGYQ ATLSSEMAAF
     HERLTPGLSA SISTIEAIYL PNDDILDQGV QAVFPYLDST VALSRNIYQE GFLPAVDILS
     STSANLNASV VGQLHSEVVL SAQNLLKQAA SLDRIVSLVG ETELSIQDKV IYERAKKLRN
     FMTQNFFVAE NQTGRKGAYV DRQTTVRDVN AILNGKLDNV SEEKLKFIGS IKEISGS
//
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