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RLMC_ECOLC
ID   RLMC_ECOLC              Reviewed;         375 AA.
AC   B1IWR3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=EcolC_2737;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) 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; CP000946; ACA78365.1; -; Genomic_DNA.
DR   RefSeq; WP_001149740.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IWR3; -.
DR   SMR; B1IWR3; -.
DR   KEGG; ecl:EcolC_2737; -.
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..375
FT                   /note="23S rRNA (uracil(747)-C(5))-methyltransferase RlmC"
FT                   /id="PRO_1000084045"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         3
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         11
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         14
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         212
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         262
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         307
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
SQ   SEQUENCE   375 AA;  41943 MW;  7D90D116EE87F0A2 CRC64;
     MQCALYDAGR CRSCQWITQP IPEQLSAKTA DLKNLLADFP VEEWCAPVSG PEQGFRNKAK
     MVVSGSVEKP LLGMLHRDGT PEDLCDCPLY PASFAPVFAA LKPFIARAGL TPYNVARKRG
     ELKYILLTES QSDGGMMLRF VLRSETKLAQ LRKALPWLQE QLPQLKVITV NIQPVHMAIM
     EGETEIYLTE QQALAERFND VPLWVRPQSF FQTNPAVASQ LYATARDWVR QLPVKHMWDL
     FCGVGGFGLH CATPDMQLTG IEIAPEAIAC AKQSAAELGL TRLQFQALDS TQFATAQGEV
     PELVLVNPPR RGIGKPLCDY LSTMAPRFII YSSCNAQTMA KDVRELPGYR IERVQLFDMF
     PHTAHYEVLT LLVKQ
 
 
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