ID A0A0G1XF47_9BACT Unreviewed; 554 AA.
AC A0A0G1XF47;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:KKU92950.1};
GN ORFNames=UY22_C0023G0002 {ECO:0000313|EMBL:KKU92950.1};
OS Candidatus Amesbacteria bacterium GW2011_GWC1_48_10.
OC Bacteria; Candidatus Amesbacteria.
OX NCBI_TaxID=1618365 {ECO:0000313|EMBL:KKU92950.1, ECO:0000313|Proteomes:UP000034877};
RN [1] {ECO:0000313|EMBL:KKU92950.1, ECO:0000313|Proteomes:UP000034877}
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:KKU92950.1}.
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DR EMBL; LCPE01000023; KKU92950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XF47; -.
DR PATRIC; fig|1618365.3.peg.599; -.
DR Proteomes; UP000034877; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 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 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;
FT DOMAIN 241..403
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 429..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 59577 MW; 9DA901D07595FB12 CRC64;
MLVKVRSVAN VGLVALPVTV EVDVAEQGFP GFTIVGLAGK AVEEARERVK TAINNSGMDF
PPKKITVNLA PADLPKDGGA YDLPMAVGIL AASGQIQDSR FMIHDSIYYG ELSLDGDLRA
TKGVLLVGLF ARSISPSNPP LTAETRAEGE KVRGGNLKGV LPEIFVPIES ANEAAVVEGI
SVFPVRNLKE LVDHLNEVSV IKSLGYLVIE DLVEDERVEY DLAEVAGQEQ AKRALTIAAA
GGHNLVMWGP PGTGKTMLAR AMPGILPPLL PAEALEVTRV YSVAGLLQPG ESLVRRRPFR
SPHHGVSAAG MIGGGSNPLP GEVSLAHLGV LFLDEMAEFP RSVLEGLRQP MEDGQVQIVR
AAAHVSYPAS FTLVAAVNPC PCGFLGHPRR ECRCSELAIR KYRGRMSGPI LDRIDLHVQV
PAVEVEKLSN APSGPPVTAK TRAGGEKVRG GRGSYDGSGD VRKKVIAARK IQEGRFKSDG
IFINSQMKNR QVRKYCPLNG ETERILRLAV EKWDLSARAY FKLIKVARTI ADLGGEKDIL
PVHMAEALQY RQMG
//