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Database: UniProt
Entry: A0A1F7QPW4_9BACT
LinkDB: A0A1F7QPW4_9BACT
Original site: A0A1F7QPW4_9BACT 
ID   A0A1F7QPW4_9BACT        Unreviewed;       476 AA.
AC   A0A1F7QPW4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=A3F37_01770 {ECO:0000313|EMBL:OGL30577.1};
OS   Candidatus Saccharibacteria bacterium RIFCSPHIGHO2_12_FULL_41_12.
OC   Bacteria; Candidatus Saccharibacteria.
OX   NCBI_TaxID=1802138 {ECO:0000313|EMBL:OGL30577.1, ECO:0000313|Proteomes:UP000177946};
RN   [1] {ECO:0000313|EMBL:OGL30577.1, ECO:0000313|Proteomes:UP000177946}
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   -!- 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:OGL30577.1}.
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DR   EMBL; MGCQ01000009; OGL30577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7QPW4; -.
DR   STRING; 1802138.A3F37_01770; -.
DR   Proteomes; UP000177946; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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   InterPro; IPR003593; AAA+_ATPase.
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; IPR005294; ATP_synth_F1_asu.
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   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   SMART; SM00382; AAA; 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   4: Predicted;
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          150..335
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   476 AA;  52046 MW;  B511D945BCE11271 CRC64;
     MSENQTNFQK IIDSGKPVGE VIGVDKFLVK VKGLHPVQIH SLVMFEDGSK GIVKQVDEQT
     VSVLHLGDET VQRGSLVGVQ HQELVTKVGK EYIGRVVSVM GKPLDGKGPI VADGTWPVFS
     PAPPLWSRKL LDKQLDSGVT TVDSIFPLVR GQRIAVLGDS KSGKTTLATQ LAINQKNTDQ
     IVVYCMIAKR RSDIDAIITK LEATGGIESA IVVVSTMFES LIMSYLAPYV AVSMAEYLWQ
     KCDQDTIIIY DDLTSHAHAC REIALLSGTS PGRDSYPGDM FYAHSSLLER AGRLESNGSC
     LTSIPIVLAA GGDITAYLPT NIMSITDGQW ILDMDVFRSG VRPAFSIGLS VTRVGGVGHN
     KRQKHIAASL MKVLALYREA EEFSHFGSEL TPESKAALEL GKNIFALLSQ GPTDVYSTYA
     QQLMLDIVME AEAGLKIDIP KLKSLANEYS EKIQKDEDYD KVRDNLKKMI LVEVKK
//
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