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Database: UniProt
Entry: B1XPZ7
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ID   RIMO_SYNP2              Reviewed;         439 AA.
AC   B1XPZ7;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   26-NOV-2014, entry version 48.
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=SYNPCC7002_A0619;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C.,
RA   Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) 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:
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; CP000951; ACA98625.1; -; Genomic_DNA.
DR   RefSeq; WP_012306249.1; NC_010475.1.
DR   RefSeq; YP_001733881.1; NC_010475.1.
DR   ProteinModelPortal; B1XPZ7; -.
DR   STRING; 32049.SYNPCC7002_A0619; -.
DR   EnsemblBacteria; ACA98625; ACA98625; SYNPCC7002_A0619.
DR   GeneID; 6055633; -.
DR   KEGG; syp:SYNPCC7002_A0619; -.
DR   PATRIC; 23815708; VBISynSp37135_0813.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224766; -.
DR   KO; K14441; -.
DR   OMA; WQGKVND; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; SSP32049:GKF7-619-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   InterPro; IPR002792; TRAM_dom.
DR   PANTHER; PTHR11918; PTHR11918; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF01938; TRAM; 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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    439       Ribosomal protein S12
FT                                methylthiotransferase RimO.
FT                                /FTId=PRO_0000375031.
FT   DOMAIN        5    116       MTTase N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   DOMAIN      372    438       TRAM. {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL        14     14       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        50     50       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL        79     79       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01865}.
FT   METAL       154    154       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01865}.
FT   METAL       158    158       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}.
SQ   SEQUENCE   439 AA;  48875 MW;  463E08FB915F9D20 CRC64;
     MTTKPTIAIS HLGCEKNRID SEHMIGLLVN AGYEVDANEE LADYVIVNTC SFIEDARAES
     VRTLVELAEA NKKIVISGCM AQHFQEQLLE ELPEAVALVG TGDYHKIVDV IQRTEQGEIV
     KEVSQEITYI ADETVPRYRT TNEAVAYLRV AEGCDYRCAF CIIPHLRGDQ RSRPIESIVA
     EAKQLAEQGV QEIILISQIT TNYGKDIYGK PKLAELLRAL GGVDVPWIRI HYAYPTGLTP
     EVIAAMRDTP NVIPYLDLPL QHSHPDILRA MNRPWQGRVN DRIIEDLKKA LPDAILRTTF
     IVGFPGETEE HFQHLVDFVK RHEFDHVGVF TFSAEEGTPA IDLPNQLPQS VKDSRRDALM
     EIQQPIAARR NELCVGQTVD VLIEQENPAT GELIGRSPRF APDVDGLVYV TGEASLGSIV
     PVQITAADIY DLYGTIVEA
//
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