ID L0GWY0_9GAMM Unreviewed; 207 AA.
AC L0GWY0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000256|ARBA:ARBA00041129, ECO:0000256|HAMAP-Rule:MF_01547};
DE EC=2.1.1.166 {ECO:0000256|ARBA:ARBA00038861, ECO:0000256|HAMAP-Rule:MF_01547};
DE AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000256|ARBA:ARBA00042745, ECO:0000256|HAMAP-Rule:MF_01547};
DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000256|ARBA:ARBA00041995, ECO:0000256|HAMAP-Rule:MF_01547};
GN Name=rlmE {ECO:0000256|HAMAP-Rule:MF_01547};
GN Synonyms=ftsJ {ECO:0000256|HAMAP-Rule:MF_01547}, rrmJ
GN {ECO:0000256|HAMAP-Rule:MF_01547};
GN ORFNames=Thimo_2549 {ECO:0000313|EMBL:AGA91273.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA91273.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA91273.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA91273.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) 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:0000256|ARBA:ARBA00037569, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00036915, ECO:0000256|HAMAP-
CC Rule:MF_01547};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. {ECO:0000256|HAMAP-
CC Rule:MF_01547}.
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DR EMBL; CP003051; AGA91273.1; -; Genomic_DNA.
DR AlphaFoldDB; L0GWY0; -.
DR STRING; 765912.Thimo_2549; -.
DR KEGG; tmb:Thimo_2549; -.
DR PATRIC; fig|765912.4.peg.2505; -.
DR eggNOG; COG0293; Bacteria.
DR HOGENOM; CLU_009422_4_0_6; -.
DR Proteomes; UP000010816; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10920:SF18; RRNA METHYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF01728; FtsJ; 1.
DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01547}; Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01547};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01547};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01547}.
FT DOMAIN 30..206
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547,
FT ECO:0000256|PIRSR:PIRSR005461-1"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
SQ SEQUENCE 207 AA; 22401 MW; A4AD3A25FD452F95 CRC64;
MAMAKTKSSR RWLDRHFNDD YVIRAQKLGY RSRAAFKLLE LQEKDRLLGR GMRVLDLGAA
PGGWSQVATQ LVGPRGIVVA LDLLAIESLP GVVILQGDFR DEAVLAELMQ ALGEAPLDVV
LSDMAPNISG IAAVDQPRAA LLGELALDCA RQVLKPGGAL VVKMFQGEGF DALLGDMRGL
FRSVAVRKPA ASRANSRECY LVAKGFR
//
