RLMC_VIBCH
ID RLMC_VIBCH Reviewed; 375 AA.
AC Q9KL20;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=VC_A0929;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003853; AAF96826.1; -; Genomic_DNA.
DR PIR; A82399; A82399.
DR RefSeq; NP_233314.1; NC_002506.1.
DR RefSeq; WP_001149813.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KL20; -.
DR SMR; Q9KL20; -.
DR STRING; 243277.VC_A0929; -.
DR DNASU; 2612926; -.
DR EnsemblBacteria; AAF96826; AAF96826; VC_A0929.
DR KEGG; vch:VC_A0929; -.
DR PATRIC; fig|243277.26.peg.3542; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_0_0_6; -.
DR OMA; YCGVGGF; -.
DR BioCyc; VCHO:VCA0929-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
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; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..375
FT /note="23S rRNA (uracil(747)-C(5))-methyltransferase RlmC"
FT /id="PRO_0000161938"
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; 42061 MW; 8B19EA3AAF4A28A9 CRC64;
MQCEFFIQKR CTSCHLCAQP YSEQVTNKDQ QLRELIAPAT DVQWLPPVTS ADTAFRNKAK
MVVLGAAHAP ILGIEDAQGQ PLSLVTCPLY PQPMQELLAY LENWIRIAGI PPYNKLKKKG
ELKFILLTRS ENSGQFMLRF VARSHAVLER IERNLPTLIA AFPMIEVISV NIQPVHMARL
EGEEEIFLTE TQSLLEHFND VPMVIRPKSF FQTNPKVAEQ LYATARTWVR EIAPTQMWDL
FCGVGGFALH CAAPDTAVTG IEIEPEAIAS AQRSAQMMGI DNLSFAALDS AKFSQSQMSA
PELVLVNPPR RGLGSELTAQ LEALAPKYIL YSSCNPQTMV KDIAELSSYQ MIRVQWFDMF
PHTDHAEVLT LLVRK
