ID   RLMB_NEIMA              Reviewed;         250 AA.
AC   Q9JUU8; A1IRE8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000255|HAMAP-Rule:MF_01887};
DE            EC=2.1.1.185 {ECO:0000255|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887};
GN   Name=rlmB {ECO:0000255|HAMAP-Rule:MF_01887}; OrderedLocusNames=NMA1127;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in 23S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01887}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:24140, Rhea:RHEA-COMP:10239, Rhea:RHEA-COMP:10241,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.185;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01887};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01887}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family. RlmB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01887}.
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DR   EMBL; AL157959; CAM08334.1; -; Genomic_DNA.
DR   PIR; B81879; B81879.
DR   RefSeq; WP_002246891.1; NC_003116.1.
DR   AlphaFoldDB; Q9JUU8; -.
DR   SMR; Q9JUU8; -.
DR   EnsemblBacteria; CAM08334; CAM08334; NMA1127.
DR   KEGG; nma:NMA1127; -.
DR   HOGENOM; CLU_021322_0_1_4; -.
DR   OMA; QVPPYEY; -.
DR   BioCyc; NMEN122587:NMA_RS05655-MON; -.
DR   Proteomes; UP000000626; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_01887; 23SrRNA_methyltr_B; 1.
DR   InterPro; IPR024915; 23S_rRNA_MeTrfase_RlmB.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR46429; PTHR46429; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..250
FT                   /note="23S rRNA (guanosine-2'-O-)-methyltransferase RlmB"
FT                   /id="PRO_0000159791"
FT   BINDING         197
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
SQ   SEQUENCE   250 AA;  27363 MW;  D44E63B33C7357BB CRC64;
     MANQRPIYGF HAVNARLWQN PKSIVELYIQ EGKSDARTRE VLEKAANENI RVYFADADRL
     NAISKGARHQ GVVGFIDASK NHVHLEDVLE NLSEPPLLLI LDGITDPHNL GACLRTADAM
     GVHAVIAPKD KSAGLNATVS KVASGAAETV PYITVTNLAR TLRELKEYGI WIIGTDMGGN
     ADLYHCDLPD SAAWVMGNEG DGMRRLTREH CDMLVSIPMF GTVESMNVSV SAGMVLSETR
     RQRVLKNEKA