ID A0A087CV99_9BIFI Unreviewed; 511 AA.
AC A0A087CV99;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:KFI87199.1};
GN ORFNames=BREU_0223 {ECO:0000313|EMBL:KFI87199.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI87199.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI87199.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI87199.1,
RC ECO:0000313|Proteomes:UP000028984};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI87199.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JGZK01000003; KFI87199.1; -; Genomic_DNA.
DR RefSeq; WP_044088416.1; NZ_JGZK01000003.1.
DR AlphaFoldDB; A0A087CV99; -.
DR STRING; 1437610.BREU_0223; -.
DR eggNOG; COG0606; Bacteria.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000028984; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028984}.
FT DOMAIN 220..403
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 511 AA; 54529 MW; A327F36ADBC5DA1E CRC64;
MAIGSTLSVG LIGLKAFIVQ VQAFISPGLP YFSIIGLPDT SLSEARERVK SACQASGFSW
PQTRVTVNMS PAAVPKRGSS HDLAIAASVL CASGAIGASC LEDTIVLGEV NLDGSVLPIH
GLLPIMLHAR ERGSNKIIVP YRNLDEAQMI EGMDVIGIRH VGELIELMGG NAVYRLPDSG
IGGEDVSDDH ALVIADRPGD MSEVLGQEHA KWALQVAAAG GHNLIMTGPP GAGKTMLASR
IPGIMSPLDE QAQLEVASIR SLCGTLPHYG ITDVPPFEAP HHTASTASLV GGGSGIAAPG
AITRAHRGIL FLDEAPEFSS RALQTLREPL ESGYVSLTRS KGSTYYPADF QLIMAANPCP
CGYYYGTGER CTCKEKERMR YFSRLSGPIL DRVDIQITVP PVSRIAQQHE SAGEPSQTIR
ARVVQARHAA AERFKPFGWS CNAQASGKWL HANTSLRAVE LVNRALANHQ LTLRGADRAM
RLAWTLADLA GRTSPTEQDV HQGIGLRTRM S
//