ID   RLMM_ACTPJ              Reviewed;         361 AA.
AC   B0BNW7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=APJL_0683;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA   Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA   Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA   Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY69252.1; -; Genomic_DNA.
DR   RefSeq; WP_005607570.1; NC_010278.1.
DR   AlphaFoldDB; B0BNW7; -.
DR   SMR; B0BNW7; -.
DR   EnsemblBacteria; ABY69252; ABY69252; APJL_0683.
DR   KEGG; apj:APJL_0683; -.
DR   HOGENOM; CLU_043780_0_0_6; -.
DR   OMA; PVDWMVC; -.
DR   OrthoDB; 902245at2; -.
DR   Proteomes; UP000008547; 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..361
FT                   /note="Ribosomal RNA large subunit methyltransferase M"
FT                   /id="PRO_1000201507"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         190
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         223..226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         262
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
SQ   SEQUENCE   361 AA;  41493 MW;  BF9646107F5F29CF CRC64;
     MNKLALYCRA GFEKETAGEI TDKAAQLGVF GFVNLKENSG YIIFECYQAG DADRLARELK
     FEQLIFARQM IVVGDMLQDL PVEDRISPIV AQYQALNPRH SSDIFVETPD TNEAKELLTF
     CRKFTVPLRN SLKKQGWLTK SERAKGSIGL HILFVRPGCC YVGYAYNDNK SPFFMGIPRL
     KFPAEAPSRS TLKLEEAILT FIPEAEEKKR FTDEMTGVDL GACPGGWTYQ LVKRGVFVYA
     VDHGKMAASL HETGRIEHCP EDGFKFQPPK RKTIDWLVCD MVEQPMRISK LIGKWLINGW
     CRETIFNLKL PMKKRYQEVQ LCLAYLEEEL EKQGFWFKIQ AKHLYHDREE ITVHIAVMGK
     R