RLME_BURCM
ID RLME_BURCM Reviewed; 220 AA.
AC Q0BGJ2;
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=Bamb_1173;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-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; CP000440; ABI86731.1; -; Genomic_DNA.
DR RefSeq; WP_011656499.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BGJ2; -.
DR SMR; Q0BGJ2; -.
DR STRING; 339670.Bamb_1173; -.
DR EnsemblBacteria; ABI86731; ABI86731; Bamb_1173.
DR GeneID; 44691854; -.
DR GeneID; 60993771; -.
DR KEGG; bam:Bamb_1173; -.
DR PATRIC; fig|339670.21.peg.389; -.
DR eggNOG; COG0293; Bacteria.
DR OMA; HRQTDHL; -.
DR Proteomes; UP000000662; Chromosome 1.
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_0000282734"
FT REGION 197..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; 24803 MW; 7430BD71E2E76A15 CRC64;
MAKNRFNQNW LHDHINDPYV KMAQREGYRA RAAYKLKEID EQDKLIRPGQ VIVDLGATPG
SWSQYARNKL AQGKKRDTQR EGGIDGTIIA LDLLPMEPIA DVHFIQGDFR EDDVLRQLED
VLEGRAVDLV ISDMAPNLSG VASADAARIE HLCDLALEFA QNHLKPDGAL LVKCFHGSGY
SQIVEKFKQQ FKVVAPRKPK ASRDKSSETF ILGRQLKQPR
