ID RIMO_RHOPB Reviewed; 441 AA. AC Q214L6; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 22-FEB-2023, entry version 106. DE RecName: Full=Ribosomal protein S12 methylthiotransferase RimO {ECO:0000255|HAMAP-Rule:MF_01865}; DE Short=S12 MTTase {ECO:0000255|HAMAP-Rule:MF_01865}; DE Short=S12 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01865}; DE EC=2.8.4.4 {ECO:0000255|HAMAP-Rule:MF_01865}; DE AltName: Full=Ribosomal protein S12 (aspartate-C(3))-methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01865}; DE AltName: Full=Ribosome maturation factor RimO {ECO:0000255|HAMAP-Rule:MF_01865}; GN Name=rimO {ECO:0000255|HAMAP-Rule:MF_01865}; OrderedLocusNames=RPC_2620; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., RA Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the methylthiolation of an aspartic acid residue of CC ribosomal protein S12. {ECO:0000255|HAMAP-Rule:MF_01865}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein CC uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L- CC aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + CC [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:37087, Rhea:RHEA-COMP:10460, Rhea:RHEA- CC COMP:10461, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:29961, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:64428, ChEBI:CHEBI:73599; EC=2.8.4.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01865}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01865}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01865}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01865}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. RimO CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01865}. 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; CP000301; ABD88170.1; -; Genomic_DNA. DR RefSeq; WP_011473066.1; NC_007925.1. DR AlphaFoldDB; Q214L6; -. DR SMR; Q214L6; -. DR STRING; 316056.RPC_2620; -. DR EnsemblBacteria; ABD88170; ABD88170; RPC_2620. DR KEGG; rpc:RPC_2620; -. DR eggNOG; COG0621; Bacteria. DR HOGENOM; CLU_018697_0_0_5; -. DR OMA; HYAYPTG; -. DR OrthoDB; 9805215at2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0103039; F:protein methylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IEA:UniProtKB-UniRule. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.80.30.20; tm_1862 like domain; 1. DR HAMAP; MF_01865; MTTase_RimO; 1. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR038135; Methylthiotransferase_N_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR005840; Ribosomal_S12_MeSTrfase_RimO. DR InterPro; IPR041582; RimO_TRAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR43837; RIBOSOMAL PROTEIN S12 METHYLTHIOTRANSFERASE RIMO; 1. DR PANTHER; PTHR43837:SF1; RIBOSOMAL PROTEIN S12 METHYLTHIOTRANSFERASE RIMO; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF18693; TRAM_2; 1. DR Pfam; PF00919; UPF0004; 1. DR SFLD; SFLDG01082; B12-binding_domain_containing; 1. DR SFLD; SFLDG01061; methylthiotransferase; 1. DR SFLD; SFLDF00274; ribosomal_protein_S12_methylth; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR TIGRFAMs; TIGR00089; radical SAM methylthiotransferase, MiaB/RimO family; 1. DR TIGRFAMs; TIGR01125; ribosomal protein S12 methylthiotransferase RimO; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..441 FT /note="Ribosomal protein S12 methylthiotransferase RimO" FT /id="PRO_0000374972" FT DOMAIN 7..117 FT /note="MTTase N-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT DOMAIN 134..371 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT DOMAIN 374..440 FT /note="TRAM" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT BINDING 16 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT BINDING 52 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT BINDING 81 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT BINDING 148 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT BINDING 152 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT BINDING 155 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" SQ SEQUENCE 441 AA; 48776 MW; 4A10D6DB6D54CDDA CRC64; MNQAAAPKVS FVSLGCPKAL VDSERIITRL RAEGYELARK HDGADLVIVN TCGFLDSAKK ESLGAIGEAM AANGKVIVTG CMGAEPEQIE AAYPNLLSIT GPQQYESVLD AVHRALPPLH NPHLDLVPAQ GIKLTPRHYA YLKISEGCNN RCSFCIIPKL RGDLVSRPAG EVLREAEKLV KAGVKELLVV SQDTSAYGVD LKYAESPWQD RNVRARFYDL AKELGELGAW VRLQYVYPYP HVDEVIGLMA QGKVLPYLDI PFQHASPEVL KQMKRPAAQD KTLARIKQWR EICPELTLRS TFIVGFPGET DSDFAYLLDW LEQAEIDRVG AFKYEAVRGA TSNALPDQVS DEVKTERWNA LMARQQKISA RRLKRKVGTR QQVIIDEVGP TVSKGRSKAD APQIDGSVYL TSRRPLRVGE IVTAKIERAD AYDLHGSVAG F //