ID A0A2T1N957_9FLAO Unreviewed; 511 AA.
AC A0A2T1N957;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:PSG88417.1};
GN ORFNames=C7H52_08940 {ECO:0000313|EMBL:PSG88417.1};
OS Aurantibacter aestuarii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aurantibacter.
OX NCBI_TaxID=1266046 {ECO:0000313|EMBL:PSG88417.1, ECO:0000313|Proteomes:UP000238426};
RN [1] {ECO:0000313|EMBL:PSG88417.1, ECO:0000313|Proteomes:UP000238426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32269 {ECO:0000313|EMBL:PSG88417.1,
RC ECO:0000313|Proteomes:UP000238426};
RA Cheng H., Wu Y.-H., Guo L.-L., Xu X.-W.;
RT "Mesoflavibacter sp. HG37 and Mesoflavibacter sp. HG96 sp.nov., two marine
RT bacteria isolated from seawater of Western Pacific Ocean.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PSG88417.1}.
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DR EMBL; PXOQ01000009; PSG88417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1N957; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000238426; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000238426}.
FT DOMAIN 213..395
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 511 AA; 56467 MW; B5F0D788A2BAE630 CRC64;
MLKKVFGSAV FGVEATTIMV EVNVDKGIGY HLVGLPDNAI KESNFRIAAA FQNNGYKIPG
KKLIINMSPA DLRKEGSAYD LTLALGILAA SDQIKSEELD KYIIMGELSL DGTLQPIKGA
LPIAIKAKEE GFKGFILPSQ NAKEAAIVDG LEVYGIDNIK QVIDFFNTGD VLEQTIINTK
EEFEKNLNFP EFDFSDVKGQ ESIKRCMEIA AAGGHNIILI GPPGAGKTML AKRLPSILPP
MTLNEALETT KIHSVVGRVK NSGLLSQRPF RSPHHTISNV ALVGGGSYPQ PGEISLSHNG
VLFLDELPEF KREVLEVMRQ PLEDREVTIS RAKFTVTYPS SFMLVASMNP SPSGYFNDPD
APVTSSPAEM QRYLSKVSGP LLDRIDIHIE VTPVPFEKLS SEQKAESSVE IRKRVTKARM
IQTKRFETSE HVHYNAQMSV KQIREYCKLD DTSLNLLKTA MERLNLSARA YDRILKVSRT
IADLDESESI TGAHISEAIQ YRSLDREGWL G
//