ID A0A0G1XDT6_9BACT Unreviewed; 510 AA.
AC A0A0G1XDT6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=UY21_C0001G0123 {ECO:0000313|EMBL:KKU92500.1};
OS Microgenomates group bacterium GW2011_GWA1_48_10.
OC Bacteria.
OX NCBI_TaxID=1618496 {ECO:0000313|EMBL:KKU92500.1, ECO:0000313|Proteomes:UP000034718};
RN [1] {ECO:0000313|EMBL:KKU92500.1, ECO:0000313|Proteomes:UP000034718}
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:KKU92500.1}.
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DR EMBL; LCPD01000001; KKU92500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XDT6; -.
DR PATRIC; fig|1618496.3.peg.126; -.
DR Proteomes; UP000034718; 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 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 217..405
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 510 AA; 55751 MW; 4DE3E41FC532C541 CRC64;
MILLIMLAKV FSGAVLGLES VPITIEVDIA SRALPHFQIV GLADKAVEES KERVRSAIQN
SSLDFPIHKI TVNLAPADLP KEGALYDLPI ALGLLLGNES LKVAISDCLF LGELSLDGGL
RSTPGVLPIA LMAKDQGFKH IFIPQVNAKE AAIISGIAIY AVPSLKDLVD HFLGVKKLVP
IPEEKLDFDF DTDYESDFSD IKGQESAKRA LEIAAAGSHN VLLKGSPGSG KTLLARTFPS
ILPKLTEDEA IEITKIYSVS NLLSLKDPVI KKRPFRSPHH TTSHIGLIGG GTRPKPGEIS
LAHRGVLFLD EIPEFPRHAL EALRQPLEDG FVTVSRASGT SHFPSKFTLI AACNPCPCGY
TLSNSRKCLC SPHQISQYQK RLSGPFLDRI DLHVFCSDIP ANKLSDYALG ENSKAIRQRV
QKARDTQIVR FNGAKITANS EMSNREVKKY CLLDEKSHQL LTQAVSTLGL SGRGYYRLLK
VSRTIADLAE SENIQVNHVA EALQYRQKDN
//