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 07-JAN-2015, entry version 63.
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};
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 -!- CATALYTIC ACTIVITY: L-aspartate-[ribosomal protein S12] + sulfur-
CC (sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-
CC aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine +
CC (sulfur carrier) + L-methionine + 5'-deoxyadenosine.
CC {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 -!- 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; WP_011503039.1; NC_007958.1.
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; CAIPSFK; -.
DR OrthoDB; EOG6P5ZD8; -.
DR BioCyc; RPAL316057:GHDC-2676-MONOMER; -.
DR Proteomes; UP000001818; Chromosome.
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
//
