ID   RLMM_ECO27              Reviewed;         366 AA.
AC   B7UHM2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=E2348C_3073;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FM180568; CAS10621.1; -; Genomic_DNA.
DR   RefSeq; WP_001045530.1; NC_011601.1.
DR   AlphaFoldDB; B7UHM2; -.
DR   SMR; B7UHM2; -.
DR   EnsemblBacteria; CAS10621; CAS10621; E2348C_3073.
DR   KEGG; ecg:E2348C_3073; -.
DR   HOGENOM; CLU_043780_0_0_6; -.
DR   OMA; PVDWMVC; -.
DR   Proteomes; UP000008205; 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_1000185318"
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;  41878 MW;  6C87F7E33A692F6D CRC64;
     MNKVVLLCRP GFEKECAAEI TDKAGQREIF GFARVKENAG YVIYECYQPD DGDKLIRELP
     FSSLIFARQW FVVGELLQHL PPEDRITPIV GMLQGVVEKG GELRVEVADT NESKELLKFC
     RKFTVPLRAA LRDAGVLANY ETPKRPVVHV FFIAPGCCYT GYSYSSNNSP FYMGIPRLKF
     PADAPSRSTL KLEEAFHVFI PADEWDERLA NGMWAVDLGA CPGGWTYQLV KRNMWVYSVD
     NGPMAQSLMD TGQVTWLRED GFKFRPTRSN ISWMVCDMVE KPAKVAALMA QWLVNGWCRE
     TIFNLKLPMK KRYEEVSHNL AYIQAQLDEH GINAQIQARQ LYHDREEVTV HVRRIWAAVG
     GRRDER