ID A0A1Q3T4H6_9CHLR Unreviewed; 551 AA.
AC A0A1Q3T4H6;
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:OJV97169.1};
GN ORFNames=BGO39_19515 {ECO:0000313|EMBL:OJV97169.1};
OS Chloroflexi bacterium 54-19.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV97169.1, ECO:0000313|Proteomes:UP000186384};
RN [1] {ECO:0000313|EMBL:OJV97169.1, ECO:0000313|Proteomes:UP000186384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54-19 {ECO:0000313|EMBL:OJV97169.1};
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:OJV97169.1}.
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DR EMBL; MKTJ01000036; OJV97169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3T4H6; -.
DR STRING; 1895928.BGO39_19515; -.
DR Proteomes; UP000186384; Unassembled WGS sequence.
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 PRINTS; PR00830; ENDOLAPTASE.
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;
FT DOMAIN 215..398
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 437..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 59798 MW; 5A7A083EDA941D4C CRC64;
MLAKVLGCAV VGLDGSLVEV EVDISNAGLP LFTVVGLPDA SVNEAKERVR SAIRNSLAIF
PMKRITVNLA PGDLRKEGPA YDLAIAVGIL LASEQLTANV ERTLFLGELS LDGTVRHTDG
ILAMVSVARR EGIRRVFVPA SDAQEAALLE DLEVYPVESL AALVRHLTGQ DPIPRHYFDP
TTLDFDNTGA DDGNDFAVIK GQEHAKRALE VAAAGGHNVI FNGPPGSGKT LLARTTVSIL
PRLSIDEALE VTKIYSVSGL LPSGMPLMRA RPFRSPHHTI SNAGLVGGGR MPRPGEISLA
HRGILFLDEL PEFGQTLLDN LRQPLEDRTL VISRASGTLA FPANFILIGA MNPCPCGFYG
DPGRACTCSP SMVTRYQKRL SGPLLDRIDI HVEVPRVEYE KLSDNRLGES SQRIRQRVEQ
AREIQRQRFK DRHAVVEPPT PIYDDESAGD EAAPAAPTKL PRSSTGPSTK PSTRQILTNS
EMGPTEIHDF CQLDTAGQAL LKAATRQLQL SARAYHRVLK LSRTIADLAG TKNIQASHLA
EAIQYRRKEA Q
//
