ID   RLME_FRATO              Reviewed;         206 AA.
AC   Q0BNB8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000255|HAMAP-Rule:MF_01547};
DE            EC=2.1.1.166 {ECO:0000255|HAMAP-Rule:MF_01547};
DE   AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547};
DE   AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547};
GN   Name=rlmE {ECO:0000255|HAMAP-Rule:MF_01547};
GN   Synonyms=ftsJ {ECO:0000255|HAMAP-Rule:MF_01547},
GN   rrmJ {ECO:0000255|HAMAP-Rule:MF_01547}; OrderedLocusNames=FTH_0425;
OS   Francisella tularensis subsp. holarctica (strain OSU18).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU18;
RX   PubMed=16980500; DOI=10.1128/jb.00506-06;
RA   Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y.,
RA   Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E.,
RA   Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.;
RT   "Chromosome rearrangement and diversification of Francisella tularensis
RT   revealed by the type B (OSU18) genome sequence.";
RL   J. Bacteriol. 188:6977-6985(2006).
CC   -!- FUNCTION: Specifically methylates the uridine in position 2552 of 23S
CC       rRNA at the 2'-O position of the ribose in the fully assembled 50S
CC       ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_01547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-
CC         methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42720, Rhea:RHEA-COMP:10202, Rhea:RHEA-COMP:10203,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.166;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01547};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01547}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01547}.
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DR   EMBL; CP000437; ABI82416.1; -; Genomic_DNA.
DR   RefSeq; WP_003014702.1; NC_017463.1.
DR   AlphaFoldDB; Q0BNB8; -.
DR   SMR; Q0BNB8; -.
DR   KEGG; fth:FTH_0425; -.
DR   OMA; HRQTDHL; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01728; FtsJ; 1.
DR   PIRSF; PIRSF005461; 23S_rRNA_mtase; 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..206
FT                   /note="Ribosomal RNA large subunit methyltransferase E"
FT                   /id="PRO_0000282747"
FT   ACT_SITE        161
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         60
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
SQ   SEQUENCE   206 AA;  23175 MW;  E14E1DA3437235BB CRC64;
     MSKGSSTKKW LHEHTSDYYV IQANKLGYRS RASFKILEIQ DKYQLFKPNM FVVDLGASPG
     GWSEQVIKYI GKNGKLIALD LLEMAPIAGV EFIQGDFSSD ETYQKLNTLV NNQKIDCVIS
     DMAPNLSGNK TSDQAKSIYL LELALDFANT NLNKNGSFVA KVFQGQGSDE YLKLVRESFN
     KVIQFKPKSS RAKSREFYVI ATEFKG