ID D5X707_THIK1 Unreviewed; 508 AA.
AC D5X707;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:ADG32154.1};
GN OrderedLocusNames=Tint_2814 {ECO:0000313|EMBL:ADG32154.1};
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG32154.1};
RN [1] {ECO:0000313|EMBL:ADG32154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 {ECO:0000313|EMBL:ADG32154.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-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; CP002021; ADG32154.1; -; Genomic_DNA.
DR AlphaFoldDB; D5X707; -.
DR STRING; 75379.Tint_2814; -.
DR KEGG; tin:Tint_2814; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_1_4; -.
DR BioCyc; TINT75379:TINT_RS14080-MONOMER; -.
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 218..400
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 508 AA; 53119 MW; 68DC500D4CF0CECF CRC64;
MSLAQVASRA LLGMEAPPVT VEVHLSPGLP GFTIVGLPEA EVREARDRVR SALINSGLGF
PSNKRIVVNL APADLPKESG RFDLPIAIGL LAAQGLIPAQ RLQGHTFAGE LSLTGALRPT
RGALAMACAL GAQGGDEAAG PRLVLPQTSA EEAALAQAVA VFGARDLQEV VAYLLEQDGA
AQPVISAKVA AAPADAPDMA EVRGHSAAKR ALEIAAAGGH HVLMVGPPGS GKSMLAQRFA
GLLPALTRAQ ALESATVLSL VGRFDPTQWG RRFVRSPHHT ASAVALVGGG AGAIRPGEIS
LATQNVLFLD ELPEFDRAVL ESLREPLETG RIHISRAARQ AEFPARFQLI AAMNPCPCGY
LGHATRACRC TPDQVSRYQG RISGPLLDRI DIQVEVGAIA PDALLQLPQG ETSAQIAARV
AIAADRQQSR QGALNAQLQG AELDEHCALD TAGSAFLSQA ITRLGWSSRA AHRVLRLART
IADLAGSQRI GLPHLAEAMQ LRRALASE
//
