ID A0A1F2VHM4_9BACT Unreviewed; 511 AA.
AC A0A1F2VHM4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:OFW44379.1};
GN ORFNames=A3J28_13465 {ECO:0000313|EMBL:OFW44379.1};
OS Acidobacteria bacterium RIFCSPLOWO2_12_FULL_60_22.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1797188 {ECO:0000313|EMBL:OFW44379.1, ECO:0000313|Proteomes:UP000178255};
RN [1] {ECO:0000313|EMBL:OFW44379.1, ECO:0000313|Proteomes:UP000178255}
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:OFW44379.1}.
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; MEKZ01000027; OFW44379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2VHM4; -.
DR Proteomes; UP000178255; 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 214..397
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 511 AA; 55579 MW; 879FBD3CDA2EA0B8 CRC64;
MFKILSAAVY GIDAYRVEVE VDLNPARDDW HFTTVGLPDA AVKESRDRVR SALRNCGYAF
PAQNITVNLA PADMKKEGSG FDLPIALGIL AGMQELAEER LSEYLFVGEL SLDGLLRPVR
GTLSIAVKAR ELGIPNLVVP AANGREAATV EGVNVFALKT LPEAVELLRA PLNFSPLRLD
VREVLEQDSS SGLDFRDVRG QTSAKRALEV SAAGGHNILM IGPPGSGKTM LAKRLATILP
HLSFEEAIQT TKVHSVAGLL DPAAGLVTAR PFRAPHHTIS DAGLIGGGAV PRPGEVSVAH
NGVLFLDELP EFPRNVLEVL RQPLEDGRVT IARAAMTISF PATFMLAAAM NPCPCGYFND
PSHECACTPP MIQRYVSKIS GPLLDRIDIH LDVPAVKYRE LRSGEAAESS AEIRARVECA
RRIQQERFAG SKIYANAQMI SRLIRKYCRL DAACEQLLET AMNRMGLSAR AHDRILKVGR
TIADLDGSPE IAPKHIAEAI QYRSLDRTYW A
//