ID A0A1Y0N009_9FLAO Unreviewed; 511 AA.
AC A0A1Y0N009;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:ARV16067.1};
GN ORFNames=BTO07_13325 {ECO:0000313|EMBL:ARV16067.1};
OS Polaribacter sp. SA4-12.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1312072 {ECO:0000313|EMBL:ARV16067.1, ECO:0000313|Proteomes:UP000195470};
RN [1] {ECO:0000313|EMBL:ARV16067.1, ECO:0000313|Proteomes:UP000195470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-12 {ECO:0000313|EMBL:ARV16067.1,
RC ECO:0000313|Proteomes:UP000195470};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP019334; ARV16067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0N009; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000195470; Chromosome.
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:UP000195470}.
FT DOMAIN 213..395
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 511 AA; 56816 MW; 47399AC0B5D9AFDF CRC64;
MLVKVYGSAV FGIEATTIIV EVNIDKGIGY HLVGLPDNAV RESSYRISAA LNNNSYKLPG
KKIIINMAPA DIRKEGASYD LTLAVGILSA SNQIKSDKID EYVIMGELSL DGSLQPIRGA
LPIAIKAREE GFKYLILPKE NAKEAAIVDE LEVLGVENIL EVINHFNGDQ KIEPTIVDTR
AEFYKNIDFP EFDFSDVKGQ ESIKRCMEIA AAGGHNIILI GPPGSGKTML AKRLPSILPP
MTLHEALETT KIHSVVGKTK KEGLLYQRPF RSPHHTISNV ALVGGGQYPR PGEISLSHNG
VLFLDELPEF KRDVLEVMRQ PLEDREVTIS RAKFTVTYPS SFMLVASMNP SPSGFFNDPN
SPMTSSPQEM QRYLSKISGP LLDRIDIHIE VTPVPFSKLS EERKGESSVD IRARVTASRE
IQSERFKDFE NVHYNAQMSV KQIREFCKLS EESKTLLKTA MEKLNLSARA YDRILKVSRT
IADLANSKDI TPDQIAEAIQ YRSLDRDGWL G
//