ID   A0A0G1L677_9BACT        Unreviewed;       507 AA.
AC   A0A0G1L677;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=UW93_C0009G0016 {ECO:0000313|EMBL:KKT91285.1};
OS   Parcubacteria group bacterium GW2011_GWC1_45_13.
OC   Bacteria.
OX   NCBI_TaxID=1618914 {ECO:0000313|EMBL:KKT91285.1, ECO:0000313|Proteomes:UP000034639};
RN   [1] {ECO:0000313|EMBL:KKT91285.1, ECO:0000313|Proteomes:UP000034639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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:KKT91285.1}.
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DR   EMBL; LCKG01000009; KKT91285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1L677; -.
DR   PATRIC; fig|1618914.3.peg.615; -.
DR   Proteomes; UP000034639; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045006; CHLI-like.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR004482; Mg_chelat-rel.
DR   InterPro; IPR025158; Mg_chelat-rel_C.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
DR   PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR   PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR   Pfam; PF13541; ChlI; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13335; Mg_chelatase_C; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          213..350
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   507 AA;  55744 MW;  E2620B644DF0F0D1 CRC64;
     MAIKLHSAEV VGLSGKIIDV EIDLSPGLFS FAIVGLADKA VAESKERISA AIKNLGARSP
     QKKNQRVVIA LAPADLKKEG PVFDLAIALS YLLASKQANF DPKNKVFLGE LALDGSLRPV
     KGVLALAEEA RRAGFSEIYV PKENGVEAAL VDGLKSFEAG SLEEILNHLE GKFPIKESRK
     TTFDLSDAVS LLDFYDVRGQ ESAKRGLEIA AAGAHNALMI GPPGTGKTML ARAFASILPP
     LSRDEALEVT KIHSIAGALK ENEFVLRHRP FRNPHHTSSY VSLVGGGTYP KPGEITLAHR
     GVLFLDEFPE FERRVIEVLR QPLEDKVVTI SRAKATLNFP AQIMMVLAMN PCPCGNMGSN
     KACVCNSAAI NRYQRKISGP IVDRIDLWLG VYGIEHKKLE DDQSPRESSA EIRKRVGLAR
     EIQKKRFVGQ NIMTNSEMSV RDIKKYCALD DESKSILQQA AARLDLSSRS YHRVIKLART
     IADLANERNI KKEHLLEALQ YRPKQLT
//