ID RIMO_CLOP1 Reviewed; 445 AA.
AC Q0TPS8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 29-MAY-2013, entry version 57.
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=CPF_1929;
OS Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / NCTC 8237 / Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA Melville S.B., Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial
RT pathogen, Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000246; ABG84692.2; -; Genomic_DNA.
DR RefSeq; YP_696362.2; NC_008261.1.
DR ProteinModelPortal; Q0TPS8; -.
DR STRING; 195103.CPF_1929; -.
DR PRIDE; Q0TPS8; -.
DR EnsemblBacteria; ABG84692; ABG84692; CPF_1929.
DR GeneID; 4202610; -.
DR KEGG; cpf:CPF_1929; -.
DR PATRIC; 19486108; VBICloPer106549_1873.
DR eggNOG; COG0621; -.
DR HOGENOM; HOG000224766; -.
DR KO; K14441; -.
DR ProtClustDB; CLSK882944; -.
DR BioCyc; CPER195103:GHAW-1945-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 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; FALSE_NEG.
PE 3: Inferred from homology;
KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW Metal-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 445 Ribosomal protein S12
FT methylthiotransferase RimO.
FT /FTId=PRO_0000374787.
FT DOMAIN 4 119 MTTase N-terminal.
FT DOMAIN 376 441 TRAM.
FT METAL 13 13 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 48 48 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 82 82 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 157 157 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 161 161 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 164 164 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
SQ SEQUENCE 445 AA; 50621 MW; 4C7720A60F18A390 CRC64;
MAKYKVGMVS LGCDKNRVDS EIMLGMVQNE YELTNNPKEA DIIIVNTCGF IEKAKQESIN
TILDMAKYKT SHNCKLLIAT GCLTQRYGDE LLELMPEIDI MLGVNDYAKI NEAIMNFING
NNEKVKATNY SDVSINEGLR LITTDKATAY LRIAEGCDNF CTYCIIPKIR GKFRSRALES
IVEEAKKLAE NGVKELILIA QDTTNYGIDI YGEKKLHLVL RELAKIEGIE WIRVLYCYPE
AIYDELIKEI SVNDKVCNYL DLPIQHISNN VLKRMGRKTT KEEIIGKIND LRKNVPNIVL
RTSLIVGFPG ESCEDFNELK DFIKTIKLDK VGVFTYSREE GTPAAIMEDQ IDEEVKKARE
EEIMLLQKEV SEEINKNKVG REYDVLIEKF NGEYYIGRSY EMAPDIDGCI YVKGNGAKKD
QFCKVKIEKA LEYDLVGVVC NESCK
//
