RLMM_SALHS
ID RLMM_SALHS Reviewed; 366 AA.
AC B4TGN7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase M {ECO:0000255|HAMAP-Rule:MF_01551};
DE EC=2.1.1.186 {ECO:0000255|HAMAP-Rule:MF_01551};
DE AltName: Full=23S rRNA (cytidine2498-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01551};
DE AltName: Full=23S rRNA 2'-O-ribose methyltransferase RlmM {ECO:0000255|HAMAP-Rule:MF_01551};
GN Name=rlmM {ECO:0000255|HAMAP-Rule:MF_01551}; OrderedLocusNames=SeHA_C3190;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
CC -!- FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42788, Rhea:RHEA-COMP:10244, Rhea:RHEA-COMP:10245,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.186;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01551};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01551}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01551}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. RlmM subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01551}.
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DR EMBL; CP001120; ACF66099.1; -; Genomic_DNA.
DR RefSeq; WP_001045499.1; NC_011083.1.
DR AlphaFoldDB; B4TGN7; -.
DR SMR; B4TGN7; -.
DR KEGG; seh:SeHA_C3190; -.
DR HOGENOM; CLU_043780_0_0_6; -.
DR OMA; PVDWMVC; -.
DR Proteomes; UP000001866; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01551; 23SrRNA_methyltr_M; 1.
DR InterPro; IPR040739; RlmM_FDX.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR011224; rRNA_MeTrfase_M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF18125; RlmM_FDX; 1.
DR PIRSF; PIRSF028774; UCP028774; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..366
FT /note="Ribosomal RNA large subunit methyltransferase M"
FT /id="PRO_1000201529"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 221..224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
SQ SEQUENCE 366 AA; 42006 MW; 61C0EFB27591CF0F CRC64;
MNKVVLLCRP GFEKECAAEI TDKAGKREIF GFARVKENAG YVIYECYQPE DGEKLISELP
FSSLIFARQW FVVGELLQHL PPEDRITPVV GMLQGVVEKG GELRVEVADT NESKELMKFC
RKFTVPLRAA LRDAGVLTNY ETPKRPVVHV FFIAPGCCYT GYSFAHNNSP FYMGIPRLKF
PSDAPSRSTL KLEEALHVFI PEDEWDERLA NGMYAVDLGA CPGGWTYQLV KRNMWVYSVD
NGPMAQSLMD TGQVTWLRED GFRYRPNRNN ISWMVCDMVE KPAKVTALMA QWLVNGWCRE
TIFNLKLPMK KRYEEVSHNL AYLQAQLDEH GVNAQIQARQ LYHDREEVTV HVRRLWAAVG
GRRDER