ID   RLMC_SHEPC              Reviewed;         389 AA.
AC   A4Y9Y4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC {ECO:0000255|HAMAP-Rule:MF_01012};
DE            EC=2.1.1.189 {ECO:0000255|HAMAP-Rule:MF_01012};
DE   AltName: Full=23S rRNA(m5U747)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01012};
GN   Name=rlmC {ECO:0000255|HAMAP-Rule:MF_01012}; Synonyms=rumB;
GN   OrderedLocusNames=Sputcn32_3054;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747
CC       (m5U747) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC         methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01012};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. RlmC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01012}.
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DR   EMBL; CP000681; ABP76767.1; -; Genomic_DNA.
DR   RefSeq; WP_011919892.1; NC_009438.1.
DR   AlphaFoldDB; A4Y9Y4; -.
DR   SMR; A4Y9Y4; -.
DR   STRING; 319224.Sputcn32_3054; -.
DR   GeneID; 45043549; -.
DR   KEGG; spc:Sputcn32_3054; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_0_0_6; -.
DR   OMA; YCGVGGF; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01012; 23SrRNA_methyltr_RlmC; 1.
DR   InterPro; IPR011825; 23SrRNA_MeTrfase_RlmC.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02085; meth_trns_rumB; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..389
FT                   /note="23S rRNA (uracil(747)-C(5))-methyltransferase RlmC"
FT                   /id="PRO_1000063008"
FT   ACT_SITE        348
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         23
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         99
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
SQ   SEQUENCE   389 AA;  43213 MW;  B056A2A6E65D8666 CRC64;
     MSAVIVNTVE QCGYFNRGQC QSCRHIQVPM AQQLMAKSLE LQQLLKPFVA PSAAIFYPPV
     TGEATAFRNK AKMVVLGAAH APVLGIVSPS GEAVSLCDCL LYPSDMQKLL HRLTQFVQQA
     GIPPYRVDKA KGELKFILLT RSQVRGEYLL RFVLRSHNSI ERIERALPTL LAEYPQINVV
     SVNIQPIHMA ILEGGEEIFL TENTRLEERF NDVPLFIRPK SFFQTNPQVA AQLYQTAREW
     VAEFAPKSLW DLFCGVGGFG LHCATKDIAL TGIEIEAEAI SCAQISANLM GLEKVQFMAL
     DSTDFAQGKN AADKPDLIIV NPPRRGIGEA LCQSLSEFAP KAILYSSCNP KTLAKDLEHI
     QGYHLTKVQL FDLFPHTDHF EVLAMLVKD