ID A0A0P7BHW3_9BACT Unreviewed; 513 AA.
AC A0A0P7BHW3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:KPM46606.1};
GN ORFNames=AFM12_18845 {ECO:0000313|EMBL:KPM46606.1};
OS Jiulongibacter sediminis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Jiulongibacter.
OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM46606.1, ECO:0000313|Proteomes:UP000050454};
RN [1] {ECO:0000313|EMBL:KPM46606.1, ECO:0000313|Proteomes:UP000050454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM46606.1,
RC ECO:0000313|Proteomes:UP000050454};
RA Liu Y., Du J., Shao Z.;
RT "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL Submitted (JUL-2015) 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:KPM46606.1}.
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; LGTQ01000016; KPM46606.1; -; Genomic_DNA.
DR RefSeq; WP_055151844.1; NZ_LGTQ01000016.1.
DR AlphaFoldDB; A0A0P7BHW3; -.
DR STRING; 1605367.AFM12_18845; -.
DR PATRIC; fig|1605367.3.peg.1215; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000050454; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050454}.
FT DOMAIN 214..397
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 513 AA; 56070 MW; 11306B3D86E968E8 CRC64;
MLATTFGAAV YGVDATLITV EISLIKGAGT SVVGLPDNAV KESLQRIDAA LKNEGYTQDR
KKTVINLAPA DIRKEGSSYD LPIALCLTTI ACGVTYAKDI SEYVILGELA LDGSLRPIKG
VLPIAIEARK QGKKGFILPK ENASEASIVN DVEIIGVESL SEAVDYLTGK INIAPLVTDT
RDIFYHTIND YEADFSHVQG QENIKRSLEI AAAGGHNAIM IGPPGAGKTM LAKRLPSILP
PLTLTEALET TKIHSVAGKL GERASLISRR PFRNPHHTIS DAALVGGGSF PQPGEISLAH
NGVLFLDELP EFKRTVLEVM RQPLEERKVS ISRTRLSVEF PSSFMLIASM NPCPCGYYNH
PEKECTCPPG AVEKYLNKVS GPLLDRIDLH VEVTPVSFDQ ISSTRKNESS EEIRKRVVAA
REVQIERFKG YSNIHSNAMM PPEMVKEICR IDEAGKALLK KAMERLGLSA RAYDRILKVS
RTIADLAGTE EIRNEQLAEA IQYRSLDREN WAG
//
