ID A0A0R2ZTL4_9PSED Unreviewed; 216 AA. AC A0A0R2ZTL4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 10-FEB-2021, entry version 19. DE RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000256|HAMAP-Rule:MF_01547}; DE EC=2.1.1.166 {ECO:0000256|HAMAP-Rule:MF_01547}; DE AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547}; DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {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=TU82_20385 {ECO:0000313|EMBL:KRP63986.1}; OS Pseudomonas orientalis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76758 {ECO:0000313|EMBL:KRP63986.1, ECO:0000313|Proteomes:UP000051716}; RN [1] {ECO:0000313|EMBL:KRP63986.1, ECO:0000313|Proteomes:UP000051716} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17489 {ECO:0000313|EMBL:KRP63986.1, RC ECO:0000313|Proteomes:UP000051716}; RA Wenning M., von Neubeck M., Huptas C., Scherer S.; RT "Two Pseudomonas sp. nov. isolated from raw milk."; RL Submitted (FEB-2015) 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|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:0000256|HAMAP-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:KRP63986.1}. 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; JYLM01000008; KRP63986.1; -; Genomic_DNA. DR RefSeq; WP_032862906.1; NZ_LT629782.1. DR EnsemblBacteria; KRP63986; KRP63986; TU82_20385. DR PATRIC; fig|76758.3.peg.5395; -. DR Proteomes; UP000051716; 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 HAMAP; MF_01547; RNA_methyltr_E; 1. DR InterPro; IPR015507; rRNA-MeTfrase_E. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01728; FtsJ; 1. DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1. DR SUPFAM; SSF53335; SSF53335; 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, ECO:0000313|EMBL:KRP63986.1}; 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, ECO:0000256|PIRSR:PIRSR005461-1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01547, ECO:0000313|EMBL:KRP63986.1}. FT DOMAIN 28..204 FT /note="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 /note="S-adenosyl-L-methionine; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547" FT BINDING 62 FT /note="S-adenosyl-L-methionine; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547" FT BINDING 80 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547" FT BINDING 96 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547" FT BINDING 121 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01547" SQ SEQUENCE 216 AA; 24111 MW; 06AF82B2E14271B0 CRC64; MARSKTSLKW LQEHFNDPYV KKAQKDGYRS RASYKLLEIQ DKDKLIRPGM SVIDLGAAPG GWSQVTSRLI GGQGRLIASD ILEMDSIPDV TFVHGDFTQD AVLAQILEAV GNSQVDLVIS DMAPNMSGLP AVDMPRAMFL CELALDLAGR VLRPGGDFLV KVFQGEGFDE YHKNIRKLFD KVQTRKPDSS RDRSREQYLL CRGFRGVEGA ASEERF //