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Database: UniProt
Entry: Q0TPS8
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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   26-NOV-2014, entry version 64.
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=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. {ECO:0000255|HAMAP-
CC       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; 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   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; CPER195103:GHAW-1945-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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   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.
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. {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   DOMAIN      376    441       TRAM. {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL        13     13       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        48     48       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        82     82       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL       157    157       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL       161    161       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL       164    164       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01865}.
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
//
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