RLME_BURCA
ID RLME_BURCA Reviewed; 220 AA.
AC Q1BXD0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Bcen_0815;
OS Burkholderia cenocepacia (strain AU 1054).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU 1054;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU 1054.";
RL Submitted (MAY-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000378; ABF75725.1; -; Genomic_DNA.
DR RefSeq; WP_006476343.1; NC_008060.1.
DR AlphaFoldDB; Q1BXD0; -.
DR SMR; Q1BXD0; -.
DR EnsemblBacteria; ABF75725; ABF75725; Bcen_0815.
DR GeneID; 56557748; -.
DR KEGG; bcn:Bcen_0815; -.
DR HOGENOM; CLU_009422_4_1_4; -.
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..220
FT /note="Ribosomal RNA large subunit methyltransferase E"
FT /id="PRO_0000282732"
FT REGION 198..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
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 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
SQ SEQUENCE 220 AA; 24787 MW; BA279619E0A9CF2D CRC64;
MAKNRFNQHW LHDHINDPYV KMAQREGYRA RAAYKLKEID EQDKLIRPGQ VIVDLGATPG
SWSQYARNKL AQGKKRDAER EGGIDGTIVA LDILPMEPIA DVHFLQGDFR EDDVLHQLEE
VLEGRAVDLV ISDMAPNLSG VASADAARIE HLCDLALEFA QNHLKPDGAL LVKCFHGSGY
SQIVEKFKQQ FKVVAPRKPK ASRDKSSETF ILGRQLKHPR