RLME_PARP8
ID RLME_PARP8 Reviewed; 220 AA.
AC B2JFN9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Bphy_0878;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC70067.1; -; Genomic_DNA.
DR RefSeq; WP_012400286.1; NZ_CADFGH010000007.1.
DR AlphaFoldDB; B2JFN9; -.
DR SMR; B2JFN9; -.
DR STRING; 391038.Bphy_0878; -.
DR EnsemblBacteria; ACC70067; ACC70067; Bphy_0878.
DR KEGG; bph:Bphy_0878; -.
DR eggNOG; COG0293; Bacteria.
DR HOGENOM; CLU_009422_4_1_4; -.
DR OMA; HRQTDHL; -.
DR OrthoDB; 1798571at2; -.
DR Proteomes; UP000001192; 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; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..220
FT /note="Ribosomal RNA large subunit methyltransferase E"
FT /id="PRO_1000194982"
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; 24678 MW; 470EC606F49DA458 CRC64;
MAKNKFNTSW LHDHINDPYV KMAQREGYRA RAAYKLKEID EQDKLIRPGQ VIVDLGAAPG
SWSQYVRNKL SQGKHRDAQR EGGIDGTIIA LDLLPMEPIA DVHFIQGDFR EDNVLAQLEE
VVGDRDVDLV ISDMAPNLSG VAVADAARIE HVCDLALEFA QNHLKPDGAL LVKCFHGSGY
SQIVEKFKHQ FKTVAARKPK ASRDKSSETF ILGRHLKRPR
