ID Q9WYY3_THEMA Unreviewed; 501 AA.
AC Q9WYY3; G4FDV8;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE SubName: Full=ComM protein {ECO:0000313|EMBL:AAD35598.1};
GN OrderedLocusNames=TM_0513 {ECO:0000313|EMBL:AAD35598.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35598.1, ECO:0000313|Proteomes:UP000008183};
RN [1] {ECO:0000313|EMBL:AAD35598.1, ECO:0000313|Proteomes:UP000008183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000313|Proteomes:UP000008183};
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., Heidelberg J.,
RA Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., Smith H.O.,
RA Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; AE000512; AAD35598.1; -; Genomic_DNA.
DR PIR; G72368; G72368.
DR RefSeq; NP_228323.1; NC_000853.1.
DR RefSeq; WP_004081420.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYY3; -.
DR PaxDb; 243274-THEMA_02110; -.
DR EnsemblBacteria; AAD35598; AAD35598; TM_0513.
DR KEGG; tma:TM0513; -.
DR KEGG; tmw:THMA_0525; -.
DR PATRIC; fig|243274.17.peg.511; -.
DR InParanoid; Q9WYY3; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000008183; 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.
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:UP000008183}.
FT DOMAIN 212..391
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 501 AA; 56046 MW; 8F2A09F10FF46D4E CRC64;
MNYNKLSSAT IQGIEAMKID VEVDFDNRSV FNDIDVVGLG DTAVKESRKR VKSAILNSGF
SLPHGKYVVN LAPGDVRKEG SMLDLPIALC ILASTGIVQV SENILAIGEL SLNGEVKRVN
GVLPVLLSLS EMFSGTVLIP KENEEEAKCV KELDIYAVES LRECVEFLRG DRTLKRIEYS
GIENTNLEYE IDFSDVRDHE MVKRAVEIAV AGFHNILMVG NPGSGKTMIA KRIPTIFPPM
SEEEILETSK VYSASGYPGI VKLRPFRAPH HTASTVSIIG GGTNPRPGEI SLAHNGVLFL
DELPEFKRDV LEALRQPLEE GIVTVARAKF TVTYPARFML VGAMNPCPCG NLGDPKQPCV
CSPRDIMRYR KKISGPLLDR MDLVINVPKL SFEEMMKKPE GEKSSSIRER VMKAREIQKR
RFRDTHISCN SQMSHRMLRR FVQLDEKSED LLKRYVERYG LSGRKIDKVL KISRTIADLE
GSNGVEMSHL AEALQYRFRE S
//
