ID D1B6D9_THEAS Unreviewed; 501 AA.
AC D1B6D9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:ACZ19580.1};
GN OrderedLocusNames=Taci_1349 {ECO:0000313|EMBL:ACZ19580.1};
OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS (Selenomonas acidaminovorans).
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19580.1, ECO:0000313|Proteomes:UP000002030};
RN [1] {ECO:0000313|EMBL:ACZ19580.1, ECO:0000313|Proteomes:UP000002030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49978 / DSM 6589 / Su883
RC {ECO:0000313|Proteomes:UP000002030};
RX PubMed=21304665; DOI=10.4056/sigs.40645;
RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT (Su883).";
RL Stand. Genomic Sci. 1:254-261(2009).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP001818; ACZ19580.1; -; Genomic_DNA.
DR RefSeq; YP_003317862.1; NC_013522.1.
DR AlphaFoldDB; D1B6D9; -.
DR STRING; 525903.Taci_1349; -.
DR EnsemblBacteria; ACZ19580; ACZ19580; Taci_1349.
DR KEGG; tai:Taci_1349; -.
DR PATRIC; fig|525903.6.peg.1350; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_1_0; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000002030; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000002030}.
FT DOMAIN 208..388
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 501 AA; 53411 MW; 1070921F9809317F CRC64;
MPLSRSMGVT LRGIEAVPVE VEVQVTGGLF AINVVGLPDA SVREARERVR GALKSLGVSL
RGRVTVNLAP AEVPKEGALL DLPMALAMMD ASGMSLPLEG SLFIGELSLD GRLRPVRGAI
PAAVLAARLG LPLILPAESA REAAMVREAR VFGASTLSQV VSHLKGERVL EQAVSPEVED
PGGDVPVDLR DVRGQAAAKR ALEVAAAGHH NLLMVGPPGS GKTMLARALK GLLPPLDDRE
MIEVLSVHSV AGLPVRSCRE RPFRPVHPTA STVAICGGGS SLRPGEVSLA HRGVLFLDEL
PEFQRDVLEA LRGPLEDGVI RVSRASGTVE YPARVLLVCS ANPCPCGYLG DPEGRCRCSL
GDVRRYRRRI SGPILDRMDM RLEVPRVPAA ELIDAPSGGE DSRMVRSRVL AARRIQADRW
GPLGYLCNSE VPEGILRRHV RLTGDAKEIL KGAIGAFRLS GRGLSRVIRL SRTVADLEGS
PSVEGRHVGE ALSYRSLEEV G
//
