ID A0A1Q2L174_9BACL Unreviewed; 513 AA.
AC A0A1Q2L174;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:AQQ54189.1};
GN ORFNames=B0X71_14465 {ECO:0000313|EMBL:AQQ54189.1};
OS Planococcus lenghuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=2213202 {ECO:0000313|EMBL:AQQ54189.1, ECO:0000313|Proteomes:UP000188184};
RN [1] {ECO:0000313|EMBL:AQQ54189.1, ECO:0000313|Proteomes:UP000188184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y42 {ECO:0000313|EMBL:AQQ54189.1,
RC ECO:0000313|Proteomes:UP000188184};
RA Yang R.;
RT "The complete genomic sequence of a novel cold adapted crude oil-degrading
RT bacterium Planococcus qaidamina Y42.";
RL Submitted (FEB-2017) 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; CP019640; AQQ54189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2L174; -.
DR KEGG; pmar:B0X71_14465; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000188184; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000188184}.
FT DOMAIN 219..399
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 269..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 56586 MW; 096FF23DD2874A95 CRC64;
MAIANYVYSV GMTGLKGQVI KVEATVRDDK EQCVIIGLPD ASIKESKERI LNCLHALNED
IDMKKITIHL SPADIRKQGT SYDAAMLLAV LQAMTKKPVV IPETTCVIAA LTLGGQLTTF
HSMIPTIHQA ILLGFKKIYI PPIDISLFAK AADSELIRMP DMPTLLAHLE GKPSLFTDDF
TLLPPEPIPE ETDNVPHVCF SAIRGHAEAK RALTLAAAGG HHVLMTGPPG CGKSLLANAF
HTILPDMTHE ELLEVYSIYQ LAKQARSLSE RPPFRSPHHS SSEGAIIGGG RHPKPGELSL
AHRGVLFLDE LGHFPRRVID TLRQPLESGF AVINRVEGSD QFPAAINLIA ATNPCPCGYY
GSNERYCTCS DKVRLKYMQK ITGPIIDRMD FVLSMKSQSV LAQSTAETSE AIRRERVTVA
RDRQRTRYGM NTTNAIVPVK LFEERAGFTE MQRKKVADIS FQEKLSSRAS LKIMRLARTI
ADLEGTEWVT DPAIEEALQW KLQAGRVHGA LIR
//