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Database: UniProt
Entry: A0A1F5GXR5_9BACT
LinkDB: A0A1F5GXR5_9BACT
Original site: A0A1F5GXR5_9BACT 
ID   A0A1F5GXR5_9BACT        Unreviewed;       398 AA.
AC   A0A1F5GXR5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:OGD96594.1};
DE   Flags: Fragment;
GN   ORFNames=A3F02_03225 {ECO:0000313|EMBL:OGD96594.1};
OS   Candidatus Curtissbacteria bacterium RIFCSPHIGHO2_12_FULL_38_9b.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1797720 {ECO:0000313|EMBL:OGD96594.1, ECO:0000313|Proteomes:UP000176666};
RN   [1] {ECO:0000313|EMBL:OGD96594.1, ECO:0000313|Proteomes:UP000176666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGD96594.1}.
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DR   EMBL; MFBJ01000021; OGD96594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5GXR5; -.
DR   Proteomes; UP000176666; 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; 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   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.
DR   PROSITE; PS50051; MCM_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          300..395
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   NON_TER         398
FT                   /evidence="ECO:0000313|EMBL:OGD96594.1"
SQ   SEQUENCE   398 AA;  43476 MW;  4465A157EE061355 CRC64;
     MLAKIISAAV IGLDAVPITV EVDIAAMGLP SFTIVGLPDK AVEESKERVR AALKNSGADF
     PPKRIIVNLA PADLPKEGPA YDLPIALGIL IASEQLSPLD LSDSIFLGEL SLDGTLRRIW
     GVLPHAIMAK EKKFKNIFIP FDNVEEARIV DKITVYPVTN LKQLFEHFAT SHLPQINRKQ
     IQSVKFKIQK YSSRSDGDYD FENIRGQENA KRALEIAAAG GHNTLMKGPP GAGKTLMARS
     FATILPKLTF EESLEVTKIY SVANLLSKDT PIIVSRPVRS PHHTTSHIGL IGGGNVPRPG
     EISLAHRGVL FLDEFPEFPR HVLEALRQPM EDGHITVSRA AGSVKFPCRF SLVAAANPCP
     CGFFQDESKP CTCSPSAITR YQKRISGPIL DRIDIHVS
//
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