ID F7YWD6_9THEM Unreviewed; 502 AA.
AC F7YWD6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:AEH51914.1};
GN ORFNames=Theth_1873 {ECO:0000313|EMBL:AEH51914.1};
OS Pseudothermotoga thermarum DSM 5069.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH51914.1, ECO:0000313|Proteomes:UP000006804};
RN [1] {ECO:0000313|EMBL:AEH51914.1, ECO:0000313|Proteomes:UP000006804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH51914.1,
RC ECO:0000313|Proteomes:UP000006804};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermotoga thermarum DSM 5069.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP002351; AEH51914.1; -; Genomic_DNA.
DR RefSeq; WP_013933122.1; NC_015707.1.
DR AlphaFoldDB; F7YWD6; -.
DR STRING; 688269.Theth_1873; -.
DR KEGG; tta:Theth_1873; -.
DR PATRIC; fig|688269.3.peg.1932; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_0_0; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000006804; Chromosome.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006804}.
FT DOMAIN 288..387
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 502 AA; 55082 MW; 140BFE4F894F8657 CRC64;
MPSKTFSATV VGLNVTKVTV EVDIDKKSVI HDVDIVGLGD TAVKESKKRV KSALKNSGFS
FPHGRIIVNL APADVKKEGS LLDLPIAVGI LQATGTINQM DLLAVGELSL EGKIRGVRGV
LTILLQLAEE NYKGIIIVPK ENIEEAQMVK GLNVYAFDEL RQVVEFVNGL VKYEPVKYLG
INSVGFESDL DFADVKGQQV AKRALEIAAA GGHNVLMKGS PGSGKTMLAR RFPTILPPLT
EQEAIEILRI YSTVMPIDGK KVTRPFRAPH HTASSVAIIG GGNDAKPGEV TLAHNGVLFL
DEFPEFRRDV IEALRQPLEE GIVTVARAKA VVTYPARFTL IAAMNPCPCG NYGDPKAVCS
CSPYDVVRYN KKVSGPILDR IDILVQVPRM DFEELFSKNV SEPSEKIRER VVKAREIQAK
RYSNYPFKTN ATIPSRLLKQ FVQLDEKSHE LLKNAAVKYS LSARSIDKIL RLSRTIADLE
SSDKVSVKHV AEALQYKIAQ ES
//
