ID A0A174HL20_9BACE Unreviewed; 512 AA.
AC A0A174HL20;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Magnesium chelatase subunit ChlI {ECO:0000313|EMBL:CUO73659.1};
GN Name=comM {ECO:0000313|EMBL:CUO73659.1};
GN ORFNames=ERS852397_02666 {ECO:0000313|EMBL:CUO73659.1};
OS Bacteroides finegoldii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=338188 {ECO:0000313|EMBL:CUO73659.1, ECO:0000313|Proteomes:UP000095517};
RN [1] {ECO:0000313|EMBL:CUO73659.1, ECO:0000313|Proteomes:UP000095517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608840 {ECO:0000313|EMBL:CUO73659.1,
RC ECO:0000313|Proteomes:UP000095517};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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; CYZH01000015; CUO73659.1; -; Genomic_DNA.
DR RefSeq; WP_055279327.1; NZ_JAKNGP010000016.1.
DR AlphaFoldDB; A0A174HL20; -.
DR STRING; 338188.ERS852397_02666; -.
DR Proteomes; UP000095517; 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:UP000095517}.
FT DOMAIN 213..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 512 AA; 56403 MW; 0960E913A1EE5915 CRC64;
MLIKVFGAAV QGIDATLITI EVNSSRGCMF YLVGLPDSAV KESHQRIISA LLVNGYKMPT
SNIVVNMAPA DIRKEGSAYD LPLAIGLLGA NETISSEKFS RYLLMGELSL DGSIQPIKGA
LPIAIKARED GFEGLIIPQQ NAREAAVVNQ LKVYGVSNIK EVVEFFNNER ELEPTVVNTR
EEFYQQQTNR DLDFADVKGQ ENVKRALEVA AAGGHNLIMV GAPGSGKSMM AKRLPSILPP
LSLGESLETT KIHSVAGQLK RGSSLISQRP FRAPHHTISQ VAMVGGGSFP QPGEISLAHN
GVLFLDELPE FNRGVLEVLR QPLEDHQITI SRIKSTISYP ANLMLIASMN PCPCGYYNHP
TKACVCSPGQ VQKYLNKISG PLLDRIDIQI EIVPVPFDKI SDQRQGEPSN IIRQRVIKAR
QLQERRYTEY AGIYCNAQMN SKLLAMYAQP DEKGLALLKN AMERFNLSAR AYDRILKVAR
TIADLEGVEQ ILPSHLAEAI SYRNLDRENW AG
//
