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RLMB_BLOFL
ID   RLMB_BLOFL              Reviewed;         254 AA.
AC   Q7VQP0;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Bfl084;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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   -!- SUBUNIT: Homodimer. {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; BX248583; CAD83607.1; -; Genomic_DNA.
DR   RefSeq; WP_011126377.1; NC_005061.1.
DR   AlphaFoldDB; Q7VQP0; -.
DR   SMR; Q7VQP0; -.
DR   STRING; 203907.Bfl084; -.
DR   EnsemblBacteria; CAD83607; CAD83607; Bfl084.
DR   KEGG; bfl:Bfl084; -.
DR   eggNOG; COG0566; Bacteria.
DR   HOGENOM; CLU_021322_0_1_6; -.
DR   OMA; QVPPYEY; -.
DR   OrthoDB; 1422015at2; -.
DR   Proteomes; UP000002192; 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; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..254
FT                   /note="23S rRNA (guanosine-2'-O-)-methyltransferase RlmB"
FT                   /id="PRO_0000159782"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT   BINDING         218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
SQ   SEQUENCE   254 AA;  28590 MW;  3EE51C5D315B7B60 CRC64;
     MSELVYGIHT VESIVNQSPN RILIVYIVSN PRDLRLKSLI YRIRKMNINI QECTRRVLNI
     KSMKSAHQGI IAEVIPMPAL NEDYLLHFLK TKNNIIPLLL VLDGITDPHN LGACIRSADA
     AGVHMIIVPR DRSANVNATV RKVASGSSDR VPFVRVTNLS RTLKLLKKYN IYIVGSVLRS
     NQILFNTRLI DPIALVMGSE SSGIRRLTRE NCDKLVHIPT LQSTVSLNVS VATGIFLFET
     VRQRKYQNGF INYS
 
 
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