ID RIMO_HELAH Reviewed; 438 AA.
AC Q17XY7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 01-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=Hac_0685;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H.,
RA Morelli G., Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied
RT a host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(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.
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DR EMBL; AM260522; CAJ99489.1; -; Genomic_DNA.
DR RefSeq; YP_664488.1; NC_008229.1.
DR ProteinModelPortal; Q17XY7; -.
DR STRING; 382638.Hac_0685; -.
DR EnsemblBacteria; CAJ99489; CAJ99489; Hac_0685.
DR GeneID; 4177361; -.
DR KEGG; hac:Hac_0685; -.
DR PATRIC; 20585277; VBIHelAci71660_0654.
DR eggNOG; COG0621; -.
DR HOGENOM; HOG000224766; -.
DR OMA; ERYHRAM; -.
DR ProtClustDB; CLSK872428; -.
DR BioCyc; HACI382638:GJAU-643-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.
PE 3: Inferred from homology;
KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW Metal-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 438 Ribosomal protein S12
FT methylthiotransferase RimO.
FT /FTId=PRO_0000374854.
FT DOMAIN 6 118 MTTase N-terminal.
FT METAL 15 15 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 49 49 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 81 81 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 150 150 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 154 154 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 157 157 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
SQ SEQUENCE 438 AA; 49548 MW; 0FAB6A25F46E7E46 CRC64;
MQKENKQLCL ISLGCSKNLV DSEVMLGKLY NYTLTNDAKS ADVILINTCG FIESAKQESI
QTILNAAKDK KEGTLLIASG CLSERYKDEI KELIPEVDIF TGVGDYDKID ILIAKKQNQF
SEQVFLSEHY NARVITGSSV HAYVKISEGC NQKCSFCAIP SFKGKLHSRE LDSILKEVED
LVLKGYKDMT FIAQDSSSFL YDKGQKDGLI QLISAIDKQQ ALRSARILYL YPSSTTLELI
GAIENSPIFQ NYFDMPIQHI SDSMLKKMRR NSSQAHHLKL LNAMKQVQES FIRSTIIVGH
PEENEGEFEE LSAFLDEFQF DRLNIFAFSA EENTHAYSLE KVPKKIINAR IKALNKIALK
HQHNSFKALL NKPIKALVEN KEGEYFYKAR DLRWAPEVDG EILINDSELN TPLKPGHYTI
VPSAFKDNIL LAKVLSPF
//
