ID RIMO_PSEE4 Reviewed; 443 AA. AC Q1I6D1; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Ribosomal protein uS12 methylthiotransferase RimO {ECO:0000255|HAMAP-Rule:MF_01865}; DE Short=uS12 MTTase {ECO:0000255|HAMAP-Rule:MF_01865}; DE Short=uS12 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01865}; DE EC=2.8.4.4 {ECO:0000255|HAMAP-Rule:MF_01865}; DE AltName: Full=Ribosomal protein uS12 (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}; GN OrderedLocusNames=PSEEN4113; OS Pseudomonas entomophila (strain L48). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=384676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L48; RX PubMed=16699499; DOI=10.1038/nbt1212; RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P., RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.; RT "Complete genome sequence of the entomopathogenic and metabolically RT versatile soil bacterium Pseudomonas entomophila."; RL Nat. Biotechnol. 24:673-679(2006). CC -!- FUNCTION: Catalyzes the methylthiolation of an aspartic acid residue of CC ribosomal protein uS12. {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; CT573326; CAK16804.1; -; Genomic_DNA. DR RefSeq; WP_011535175.1; NC_008027.1. DR AlphaFoldDB; Q1I6D1; -. DR SMR; Q1I6D1; -. DR STRING; 384676.PSEEN4113; -. DR GeneID; 32807128; -. DR KEGG; pen:PSEEN4113; -. DR eggNOG; COG0621; Bacteria. DR HOGENOM; CLU_018697_0_0_6; -. DR OrthoDB; 9805215at2; -. DR Proteomes; UP000000658; Chromosome. 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: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_uS12_MeSTrfase_RimO. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR NCBIfam; TIGR01125; 30S ribosomal protein S12 methylthiotransferase RimO; 1. DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1. 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; SFLDS00029; Radical_SAM; 1. DR SFLD; SFLDF00274; ribosomal_protein_S12_methylth; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 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..443 FT /note="Ribosomal protein uS12 methylthiotransferase RimO" FT /id="PRO_0000374944" FT DOMAIN 8..118 FT /note="MTTase N-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT DOMAIN 137..375 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT DOMAIN 378..443 FT /note="TRAM" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01865" FT BINDING 17 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 53 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 82 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 151 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" FT BINDING 158 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 443 AA; 49408 MW; 55EF840663A08828 CRC64; MSTTPATPKV GFVSLGCPKA LVDSERILTQ LRMEGYEVVP TYEDADVVVV NTCGFIDSAK AESLEVIGEA IKENGKVIVT GCMGVEEGSI RDVHPSVLSV TGPQQYEQVV NAVHEVVPPR QDHNPLIDLV PPQGVKLTPR HYAYLKISEG CNHSCSFCII PSMRGKLVSR PVGEVLSEAE RLVKAGVKEI LVISQDTSAY GVDVKYKTDF WNGRPVKTRM LELCEALSSL GAWVRLHYVY PYPNVDDVIP LMAAGKILPY LDIPFQHASP KVLKSMKRPA FEDRTLARIK NWREQCPELV IRSTFIVGFP GETEEDFQYL LDWLTEAQLD RVGCFQYSPV EGAPANDLGL DEVPDDVKQE RWDRFMAHQQ AISAARLQQR IGKEIEVLID EVEEQGSVGR SFFDAPEIDG SVFIDGDHGF KPGDKVRCRI VDADEYDMWA EPI //