ID RIMO_SHESA Reviewed; 480 AA.
AC A0L1C8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 29-MAY-2013, entry version 55.
DE RecName: Full=Ribosomal protein S12 methylthiotransferase RimO;
DE Short=S12 MTTase;
DE Short=S12 methylthiotransferase;
DE EC=2.-.-.-;
DE AltName: Full=Ribosome maturation factor RimO;
GN Name=rimO; OrderedLocusNames=Shewana3_3627;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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.
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DR EMBL; CP000469; ABK49847.1; -; Genomic_DNA.
DR RefSeq; YP_871253.1; NC_008577.1.
DR ProteinModelPortal; A0L1C8; -.
DR STRING; 94122.Shewana3_3627; -.
DR EnsemblBacteria; ABK49847; ABK49847; Shewana3_3627.
DR GeneID; 4476226; -.
DR KEGG; shn:Shewana3_3627; -.
DR PATRIC; 23575266; VBISheSp134792_3998.
DR eggNOG; COG0621; -.
DR HOGENOM; HOG000224766; -.
DR KO; K14441; -.
DR OMA; RVDTEHM; -.
DR ProtClustDB; PRK14862; -.
DR BioCyc; SSP94122:GJ9K-3740-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:HAMAP.
DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR GO; GO:0016740; F:transferase activity; IEA:HAMAP.
DR GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IEA: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 1 480 Ribosomal protein S12
FT methylthiotransferase RimO.
FT /FTId=PRO_0000375005.
FT DOMAIN 37 147 MTTase N-terminal.
FT DOMAIN 405 471 TRAM.
FT METAL 46 46 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 82 82 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 111 111 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 179 179 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 183 183 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 186 186 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
SQ SEQUENCE 480 AA; 53567 MW; F189346A0B984BCF CRC64;
MTVETFNPKQ TTTLETPAKT LEAASADLAN AESATGNRIG FVSLGCPKNL VDSERILTQL
RIDGYEVTNS YDNADLVIVN TCGFIDAAVE ESLDAVREAL EENGKVIVTG CLGAKENQIR
EVHPDVLEIT GPHSYEAVLK HVHKYVPKPE HNPFTSLIPQ TGVKLTPKHY AYLKISEGCD
NRCTFCIIPA LRGDLDSRPA GSVLDEAKRL VESGVQEILV VSQDTSAYGK DKGGRTDFWN
GMPVKQDITS LARQLGKMGA WVRLHYIYPY PWVDDLIPLM AEGLILPYLD IPMQHASPRI
LKMMKRPGRV DRQLEAIQRW REICPDLVIR STFIVGFPGE TEEDFEMLLD FLREARLDRV
GCFKYSEVEG AVANTIAELI SEDVKEDRYH RFMEVQAEIS AERLARFVGR TMDILIDDVD
EEGAIGRSFA DAPEIDGMVF INGETELEPG MLVRAVITHS DEHDLWAELV DADAEDDIEA
//
