ID   RLME_EHRCJ              Reviewed;         171 AA.
AC   Q3YRW8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase E;
DE            EC=2.1.1.166;
DE   AltName: Full=23S rRNA Um2552 methyltransferase;
DE   AltName: Full=rRNA (uridine-2'-O-)-methyltransferase;
GN   Name=rlmE; Synonyms=ftsJ, rrmJ; OrderedLocusNames=Ecaj_0501;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(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:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. {ECO:0000305}.
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DR   EMBL; CP000107; AAZ68537.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3YRW8; -.
DR   SMR; Q3YRW8; -.
DR   STRING; 269484.Ecaj_0501; -.
DR   EnsemblBacteria; AAZ68537; AAZ68537; Ecaj_0501.
DR   KEGG; ecn:Ecaj_0501; -.
DR   eggNOG; COG0293; Bacteria.
DR   HOGENOM; CLU_009422_4_4_5; -.
DR   OMA; FRSTEYH; -.
DR   Proteomes; UP000000435; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProt.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 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; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..171
FT                   /note="Ribosomal RNA large subunit methyltransferase E"
FT                   /id="PRO_0000155493"
FT   ACT_SITE        123
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         22
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   171 AA;  19554 MW;  0E612275C3E07A66 CRC64;
     MDNKFSIFKK GQYVLDLGSF PGGWSQFAAQ KVSHGNNNLV FSVDIQNMDA IPNVIFIKCD
     ISNEIEILND KFHNKKFDVI LSDMAPKACG NKQVDHANII NLCEMSLDIV IKFARENGTF
     ITKILQGEYE KEFYQSMKSN FKLVKYFKPK ASRKDSSEIY LVGLGFKKDF Q