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 16-JUN-2009, entry version 29. DE RecName: Full=Ribosomal protein S12 methylthiotransferase rimO; DE Short=S12 methylthiotransferase; DE Short=S12 MTTase; DE EC=2.-.-.-; DE AltName: Full=Ribosome maturation factor rimO; GN Name=rimO; OrderedLocusNames=RPC_2620; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Anderson I., Oda Y., Harwood C.S., 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 CC residue of ribosomal protein S12 (By similarity). CC -!- COFACTOR: Binds 2 4Fe-4S clusters. One cluster is coordinated with CC 3 cysteines and an exchangeable S-adenosyl-L-methionine (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the methylthiotransferase family. RimO CC subfamily. CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain. CC -!- SIMILARITY: Contains 1 TRAM domain. 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; YP_532489.1; -. DR GeneID; 3973299; -. DR GenomeReviews; CP000301_GR; RPC_2620. DR KEGG; rpc:RPC_2620; -. DR HOGENOM; Q214L6; -. DR OMA; Q214L6; LGAWVRL. DR BioCyc; RPAL316056:RPC_2620-MON; -. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR HAMAP; MF_01865; -; 1. DR InterPro; IPR005840; CHP01125. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; Radical_SAM. DR InterPro; IPR002792; TRAM. DR InterPro; IPR005839; UPF0004. DR InterPro; IPR013848; UPF0004_N. DR PANTHER; PTHR11918; UPF0004; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR01125; CHP1125; 1. DR TIGRFAMs; TIGR00089; UPF0004; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 441 Ribosomal protein S12 FT methylthiotransferase rimO. FT /FTId=PRO_0000374972. FT DOMAIN 7 117 MTTase N-terminal. FT DOMAIN 374 440 TRAM. FT METAL 16 16 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 52 52 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 81 81 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 148 148 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 152 152 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 155 155 Iron-sulfur (4Fe-4S-S-AdoMet) (By FT similarity). 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 //