ID A0A1T4MAN5_9GAMM Unreviewed; 206 AA.
AC A0A1T4MAN5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=BTE48_04185 {ECO:0000313|EMBL:OPX56184.1};
OS Oceanospirillum multiglobuliferum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Oceanospirillum.
OX NCBI_TaxID=64969 {ECO:0000313|EMBL:OPX56184.1, ECO:0000313|Proteomes:UP000191418};
RN [1] {ECO:0000313|EMBL:OPX56184.1, ECO:0000313|Proteomes:UP000191418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33336 {ECO:0000313|EMBL:OPX56184.1,
RC ECO:0000313|Proteomes:UP000191418};
RA Carney J.G., Trachtenberg A.M., Rheaume B.A., Linnane J.D., Pitts N.L.,
RA Mykles D.L., Maclea K.S.;
RT "Genome Sequencing of a Marine Spirillum, Oceanospirillum multiglobuliferum
RT ATCC 33336, from Japan.";
RL Submitted (JAN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPX56184.1}.
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DR EMBL; MTSM01000004; OPX56184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4MAN5; -.
DR STRING; 64969.SAMN02745127_00728; -.
DR OrthoDB; 9790080at2; -.
DR Proteomes; UP000191418; Unassembled WGS sequence.
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:UP000191418};
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 28..204
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547,
FT ECO:0000256|PIRSR:PIRSR005461-1"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
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 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547"
SQ SEQUENCE 206 AA; 22666 MW; 1A7A1CCE305CB85A CRC64;
MARSKTSQKW LDEHVNDPYV KKAQMDGYRS RASYKLIEIN EKDKLYRSGS VVMDLGSAPG
GWSQVVAPVV GESGRVIASD ILPMDGLDGV TFIQGDFTDE AVYEEIIQAL EGDQVDTVIS
DMAPNMSGVN TTDQYASMYL VELALDMARN VLKPGGSFCA KVFQGVGYEE YVKDVRSSFD
KVIVRKPAAS RPRSREVYLV GKGFKG
//
