RLMM_XANC5
ID RLMM_XANC5 Reviewed; 347 AA.
AC Q3BX58;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=XCV0924;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ22555.1; -; Genomic_DNA.
DR RefSeq; WP_011346493.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BX58; -.
DR SMR; Q3BX58; -.
DR STRING; 456327.BJD11_18165; -.
DR EnsemblBacteria; CAJ22555; CAJ22555; XCV0924.
DR KEGG; xcv:XCV0924; -.
DR eggNOG; COG2933; Bacteria.
DR HOGENOM; CLU_043780_0_0_6; -.
DR OMA; PVDWMVC; -.
DR Proteomes; UP000007069; 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..347
FT /note="Ribosomal RNA large subunit methyltransferase M"
FT /id="PRO_0000314549"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 217..220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
SQ SEQUENCE 347 AA; 38998 MW; C754AD849DD9FB55 CRC64;
MSGLVCYCRQ GFEPELAAEL SARAAFVGIA GYARTQRNDG YVLFVCDEAA QLAAKLQWRE
LIFARQKLVV IAELKGIDPK DRITPILAAL DGHQRFGDLW VEHPDSDAGK PLAGLARSFG
NALRPALRKA GLLTDKPQLR QPRLHVCFLD GDHAVLAVAD NADSAPWPLG IPRLKLLPEA
PSRSALKLDE ALLTLLTPEE RDALVKPGMR AADLGAAPGG WTWVLTRQHV HVTSVDNGPL
REHVLETGLV EHLRADGFHW KPAQPLDWMV CDMVEQPRRV AERMATWVRE GWCRNTIFNL
KLPMKKRWDE TRLCLDLFEQ QAEKSLIVRA KQLYHDREEI TVLAMRE
