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Database: UniProt
Entry: Q136X7
LinkDB: Q136X7
Original site: Q136X7 
ID   RIMO_RHOPS              Reviewed;         441 AA.
AC   Q136X7;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   01-OCT-2014, entry version 60.
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.-.-.- {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=RPD_2633;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
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.,
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   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01865}.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters. One cluster is coordinated with
CC       3 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   -!- SIMILARITY: Contains 1 MTTase N-terminal domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01865}.
CC   -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01865}.
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DR   EMBL; CP000283; ABE39862.1; -; Genomic_DNA.
DR   RefSeq; YP_569763.1; NC_007958.1.
DR   ProteinModelPortal; Q136X7; -.
DR   STRING; 316057.RPD_2633; -.
DR   EnsemblBacteria; ABE39862; ABE39862; RPD_2633.
DR   GeneID; 4023130; -.
DR   KEGG; rpd:RPD_2633; -.
DR   PATRIC; 23280305; VBIRhoPal120395_2718.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224766; -.
DR   KO; K14441; -.
DR   OMA; PHDPFID; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; RPAL316057:GHDC-2676-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01865; MTTase_RimO; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR023970; MeThioTfrase/rSAM.
DR   InterPro; IPR005839; Methylthiotransferase.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR005840; Ribosomal_S12_MeSTrfase_RimO.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR002792; TRAM_dom.
DR   PANTHER; PTHR11918; PTHR11918; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00089; TIGR00089; 1.
DR   TIGRFAMs; TIGR01125; TIGR01125; 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_0000374973.
FT   DOMAIN        7    117       MTTase N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   DOMAIN      374    440       TRAM. {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL        16     16       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        52     52       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        81     81       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL       148    148       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL       152    152       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL       155    155       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01865}.
SQ   SEQUENCE   441 AA;  48818 MW;  726C7C07A20B7ACC CRC64;
     MQQAAAPKIS FVSLGCPKAL VDSERIITRL RAEGYELARQ HDGADLVIVN TCGFLDSAKQ
     ESLAAIGEAM AANGKVIVTG CMGAEPEQIE AAYPGVLSIT GPQQYESVLE AVHRAKPALH
     NPHLDLVPEQ GIRLTPRHYA YLKISEGCNN RCSFCIIPKL RGDLVSRSAD DVLREAEKLV
     AAGVKELLVI SQDTSAYGVD LKYAESPWKD RTVRAKFIDL ARELGELGAW VRLHYVYPYP
     HVDEVIGLMA EGKVLPYLDI PFQHASPDVL KLMKRPAAQD KTLDRIKRWR ADCPDLALRS
     TFIVGFPGET ERDFEFLLDW LDEAEIDRLG AFKYEPVAGA PSNALPDQIS AEVKQERWNR
     LMARQQVISA RRLKRKVGTR QQIIIDEVGP TVAKGRSKAD APEIDGSVYL SSRRPLRVGE
     IVTAKIDRAD AYDLHGTVAG F
//
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