ID A0A1F5Y3D7_9BACT Unreviewed; 509 AA.
AC A0A1F5Y3D7;
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:OGF94717.1};
GN ORFNames=A2Y47_00545 {ECO:0000313|EMBL:OGF94717.1};
OS Candidatus Giovannonibacteria bacterium RIFCSPLOWO2_12_43_8.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1798361 {ECO:0000313|EMBL:OGF94717.1, ECO:0000313|Proteomes:UP000177720};
RN [1] {ECO:0000313|EMBL:OGF94717.1, ECO:0000313|Proteomes:UP000177720}
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:OGF94717.1}.
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DR EMBL; MFIN01000042; OGF94717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5Y3D7; -.
DR Proteomes; UP000177720; 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 213..392
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 509 AA; 56570 MW; C45F13CE5A195EBB CRC64;
MSAAKTHSAE ILGLEGEIID VEVDLAPGLF HFSIVGLPDK AVEESRERVS SAIKNTGLRH
PQKKNQRVVV SLAPADLKKE GPLFDLAIAV GYLMASKQIE FDSSKKLFLG ELALDGSLRK
IKGALSLAMA AKEAGFQEII LPRENAPEAS LVDGIRTYGM GSLSQVLKYL KGEEKIEPSA
ATKIETENLY SLDFGEIKGQ ETAKRGLALA AAGAHHVLMV GPPGTGKTML ARALPSILPP
MNFEEVLEVT KIHSVSGNLR KSYVSERPFR NPHHTASYVA LVGGGQVPRP GEITLAHRGV
LFLDEFPEFE RRVLEALRQP LEDGEITISR AKGTLTFPAR SLTVFAMNPC PCGNYGSDKK
PCLCTTQTLY RYQRKVSGPI ADRIDIWLEV PHFEHEKMSL KSKQESDTIQ KKVIRVREIQ
KERFAKRDIS LNSHMRPKDL EEFAPLSAET QEIMHTAAKK LDLSARAYHR VIKLARTVAD
FEGSRDIKKE HILEAIQYRP RKNFFVYET
//
