ID A0A1Q3QPC7_9BACT Unreviewed; 530 AA.
AC A0A1Q3QPC7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:OJV41366.1};
GN ORFNames=BGO25_16720 {ECO:0000313|EMBL:OJV41366.1};
OS Acidobacteriales bacterium 59-55.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales.
OX NCBI_TaxID=1895690 {ECO:0000313|EMBL:OJV41366.1, ECO:0000313|Proteomes:UP000186822};
RN [1] {ECO:0000313|EMBL:OJV41366.1, ECO:0000313|Proteomes:UP000186822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=59-55 {ECO:0000313|EMBL:OJV41366.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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}.
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:OJV41366.1}.
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; MKSV01000007; OJV41366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3QPC7; -.
DR STRING; 1895690.BGO25_16720; -.
DR Proteomes; UP000186822; 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}.
FT DOMAIN 220..403
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 530 AA; 57710 MW; 28279F65B0049DB2 CRC64;
MLFTARSAAV YGIDAHIIDV EVDFSGVKLD KELFNTVGLP DAAVRESRDR VRSAIKNSGF
DIPPTRITIN LAPADLKKEG SGFDLPIAIG ILGAYGALHI KDLSDFLLVG ELGLDGSLRA
VQGMLPIAVA ARAKGIPNLV IPASNAREAA VVEGVNVYPV KSLLEVRELL NAAAFGTVTA
VPLKVETANL LNEMQHFPFD FKDVRGQHVA KRALEVAAAG GHNILMIGPP GSGKTMLAKR
LPSILSPLRF EEALETTKIH SVAGVLDAEQ GLVTHRPFRS PHHTISDAGL IGGGMMPRPG
EVSLAHNGLL FLDELPEFPR NVLEVMRQPL EDGMVTIARA AMSLSFPARF MLAAAMNPCP
CGYFNDKSRE CMCTPPMIQR YVSKVSGPLL DRIDIHIEVP AVQYKELRGG AAAEGSEEIR
NRVLAARELQ HERFSEAGER TNGSAKVASR QIFANSQMNT RQIRTYCELS SEAERLLERA
MQQQGLSARA HDRILKVART IADLGRDQDI GVKHIAEAIQ YRTLDRSYWS
//