(data stored in ACNUC7421 zone)

SWISSPROT: RIMO_LEGPC

ID   RIMO_LEGPC              Reviewed;         439 AA.
AC   A5IGM4;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 82.
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}; OrderedLocusNames=LPC_2609;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylthiolation of an aspartic acid residue of
CC       ribosomal protein S12. {ECO:0000255|HAMAP-Rule:MF_01865}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein
CC         uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-
CC         aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine +
CC         [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:37087, Rhea:RHEA-COMP:10460, Rhea:RHEA-
CC         COMP:10461, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:29961,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64428, ChEBI:CHEBI:73599; EC=2.8.4.4;
CC         Evidence={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}.
DR   EMBL; CP000675; ABQ56524.1; -; Genomic_DNA.
DR   RefSeq; WP_011945836.1; NC_009494.2.
DR   PRIDE; A5IGM4; -.
DR   EnsemblBacteria; ABQ56524; ABQ56524; LPC_2609.
DR   KEGG; lpc:LPC_2609; -.
DR   HOGENOM; HOG000224766; -.
DR   KO; K14441; -.
DR   OMA; CLSERYK; -.
DR   BioCyc; LPNE400673:LPC_RS03880-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0103039; F:protein methylthiotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.12160; -; 1.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01865; MTTase_RimO; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR005839; Methylthiotransferase.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR038135; Methylthiotransferase_N_sf.
DR   InterPro; IPR005840; Ribosomal_S12_MeSTrfase_RimO.
DR   InterPro; IPR041582; RimO_TRAM.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR002792; TRAM_dom.
DR   PANTHER; PTHR43837; PTHR43837; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF18693; TRAM_2; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SFLD; SFLDF00274; ribosomal_protein_S12_methylth; 1.
DR   SFLD; SFLDG01061; methylthiotransferase; 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;
DR   PRODOM; A5IGM4.
DR   SWISS-2DPAGE; A5IGM4.
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..439
FT                   /note="Ribosomal protein S12 methylthiotransferase RimO"
FT                   /id="PRO_0000374873"
FT   DOMAIN          3..113
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
FT   DOMAIN          370..436
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
FT   METAL           12
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
FT   METAL           48
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
FT   METAL           77
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
FT   METAL           144
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
FT   METAL           148
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
FT   METAL           151
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01865"
SQ   SEQUENCE   439 AA;  48988 MW;  2FE348CA21BC7491 CRC64;
     MNHKVGFVSL GCPKALVDSE RIITQLKAQG YELVPTYEDA GVVVINTCGF IDSAVQESLD
     TIKEAMAENG RVIVTGCLGA KADVIKNACP DVLHISGAHA YEEVVNAVHQ HLPPPADPFT
     QLIPPQGIKL TPRHYAYLKI SEGCNQKCTF CIIPTMRGKL QSYPMAQILT EAKKLKQAGV
     KELLVISQDT SAYGVDTRYQ QVEWQGKTVN TRFYDLCEQL GELGIWVRLH YVYPYPHVDD
     IVPLMRDGLI LPYLDIPLQH ANSRILKAMK RPASSENTLL RIASWREICP DITLRSTFIV
     GFPGETEEEF SELLAFLKEA QLDRVGCFKY SPVEGAKAND LDNPVSEDIK EERYHRFMQV
     QAEISRNKLK NKIGSTQTVL IDEITEDQII ARSKSDAPEI DGLVYLPKIS GITVGSFAEA
     MITDSDDYDL YGDLEYSLA
//

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