ID   A0A1M5D028_9BACE        Unreviewed;       512 AA.
AC   A0A1M5D028;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Magnesium chelatase family protein {ECO:0000313|EMBL:SHF60274.1};
GN   ORFNames=SAMN05444405_11115 {ECO:0000313|EMBL:SHF60274.1};
OS   Bacteroides luti.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHF60274.1, ECO:0000313|Proteomes:UP000184509};
RN   [1] {ECO:0000313|EMBL:SHF60274.1, ECO:0000313|Proteomes:UP000184509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26991 {ECO:0000313|EMBL:SHF60274.1,
RC   ECO:0000313|Proteomes:UP000184509};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQTV01000011; SHF60274.1; -; Genomic_DNA.
DR   RefSeq; WP_073402173.1; NZ_FQTV01000011.1.
DR   AlphaFoldDB; A0A1M5D028; -.
DR   STRING; 1297750.SAMN05444405_11115; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000184509; 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:UP000184509}.
FT   DOMAIN          213..396
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   512 AA;  56057 MW;  3CDEB420ECE42702 CRC64;
     MLVKVFGAAV QGIDATVITI EVNSTRGCMF HLVGLPDSAV KESHERILSA LQVNGYKFPT
     SQIVINMAPA DIRKEGSAYD LPLAIGMMAA KENVSTEKLG KYIIMGELSL DGSLQTIKGA
     LPIAIKAREE GYEGLIVPRQ NAKEAAVVNN LKVYGANNIK EVMGFFNGEE TLEQTVVNTR
     EEFYAQQTSF EFDFSDVKGQ ENVKRSLEVA AAGGHNLIMI GAPGSGKSMM AKRLPSILPP
     LSLGESLETT KIHSVAGKLG KDTSLIAKRP FRSPHHTISQ VAMVGGGAYP QPGEISLAHN
     GLLYLDELAE FNRSVLEVLR QPLEDRTISV SRAKYSIDYP AGFMMIASMN PCPCGYYNHP
     TKACVCSSGQ VQKYLNRISG PLLDRIDIQV EIVPVPFEKI SDKRTSEPSS AIRERVIKAR
     QIQEQRYADY PGVYCNAQMS TKLLHTFAEP DSTGLTLLKN AMNRLNLSAR AYDRILKVSR
     TIADLDGSEK VKSAHLAEAI SYRNLDRESW AG
//