ID D2Q9I0_BIFDB Unreviewed; 508 AA.
AC D2Q9I0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=ATPase-like magnesium chelatase subunit ChlI {ECO:0000313|EMBL:ADB09466.1};
DE EC=6.6.1.1 {ECO:0000313|EMBL:ADB09466.1};
GN OrderedLocusNames=BDP_0806 {ECO:0000313|EMBL:ADB09466.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09466.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB09466.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP001750; ADB09466.1; -; Genomic_DNA.
DR RefSeq; WP_003840732.1; NC_013714.1.
DR AlphaFoldDB; D2Q9I0; -.
DR STRING; 401473.BDP_0806; -.
DR GeneID; 69536985; -.
DR KEGG; bde:BDP_0806; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_0_11; -.
DR Proteomes; UP000008693; 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:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0032508; P:DNA duplex unwinding; 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; 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 Ligase {ECO:0000313|EMBL:ADB09466.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT DOMAIN 217..400
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 508 AA; 54420 MW; 865195DB89187E32 CRC64;
MAIGSALSVG LIGLKAFIIQ IQAFISPGLP YFSIIGLPDT SLSEAKERVK SACQASGFKW
PETRVTVNLS PASMPKKGSS HDLAIAASVL SASGTIGHDC LADTIVLGEV NLDGTVLPVN
GLLPIMLHAR EQGIRQVIVP HANIDEARLI DDIDVIGVRH VGELIELMGG HATYHIPDTQ
RDIGTGMDVT QCSAPGDMCE VVGQESTKWA LEVAAAGGHH LLMTGPPGTG KTMLASRMPG
IMSPLNETEQ LEIASIRSLC GTLPSYGITD VPPFEAPHHT ASMASLVGGG TGLAQPGAIT
RAHRGILFMD EAPEFSARAL QTLREPLESG YVAISRSKGT TYYPARFQLI MAANPCPCGF
SYGNGERCAC KEKDRIKYFS RLSGPILDRI DIQVEVLPVD RIDSGSRQTG ESSHTIRLRV
MVARQMAQER FREYGWSCNA QATGTWLRAN TSHKAIALVN RALASERLSL RGADRAMRLA
WTLADLAGKS SPGPTEMMQG ISMRTRLS
//