ID   RLME_METFK              Reviewed;         207 AA.
AC   Q1H387;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Mfla_0782;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000284; ABE49050.1; -; Genomic_DNA.
DR   RefSeq; WP_011479147.1; NC_007947.1.
DR   AlphaFoldDB; Q1H387; -.
DR   SMR; Q1H387; -.
DR   STRING; 265072.Mfla_0782; -.
DR   PRIDE; Q1H387; -.
DR   EnsemblBacteria; ABE49050; ABE49050; Mfla_0782.
DR   KEGG; mfa:Mfla_0782; -.
DR   eggNOG; COG0293; Bacteria.
DR   HOGENOM; CLU_009422_4_0_4; -.
DR   OMA; HRQTDHL; -.
DR   OrthoDB; 1798571at2; -.
DR   Proteomes; UP000002440; Chromosome.
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; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..207
FT                   /note="Ribosomal RNA large subunit methyltransferase E"
FT                   /id="PRO_0000282762"
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   207 AA;  23199 MW;  3CFBA71A7A29517A CRC64;
     MKRRPTSKAW LQEHVNDEFV KRAQRDGYRA RAAYKLLEID DKDQLIKPGM TIVDLGSAPG
     SWSQVAVQRL AGQGRVIALD ILEMPPIPGV EFIQGDFREE EILLVLEKSL NGKPVDLVIA
     DMAPNISGIS DVDQARAAYL VELALEFSRE WLKPGGNFLV KVFVGSGFDE IVMAMRDSFE
     KVVTRKPKAS RDRSSEVYLL GLKRRNA