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RLME_PSYA2
ID   RLME_PSYA2              Reviewed;         210 AA.
AC   Q4FQX1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=Psyc_1739;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19587.1; -; Genomic_DNA.
DR   RefSeq; WP_011281000.1; NC_007204.1.
DR   AlphaFoldDB; Q4FQX1; -.
DR   SMR; Q4FQX1; -.
DR   STRING; 259536.Psyc_1739; -.
DR   EnsemblBacteria; AAZ19587; AAZ19587; Psyc_1739.
DR   KEGG; par:Psyc_1739; -.
DR   eggNOG; COG0293; Bacteria.
DR   HOGENOM; CLU_009422_4_0_6; -.
DR   OMA; HRQTDHL; -.
DR   OrthoDB; 1798571at2; -.
DR   Proteomes; UP000000546; 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   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..210
FT                   /note="Ribosomal RNA large subunit methyltransferase E"
FT                   /id="PRO_0000155526"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
SQ   SEQUENCE   210 AA;  23319 MW;  151CEE7804AF0CC1 CRC64;
     MATRIENKKL SKSSSAWMKE HIDDHYVQKA QKDGYRARAA YKLLEINEKT NLIKKGMTVV
     DLGSAPGSWS QVAGQLVGEK GILIASDILP MDTLPDVTFI QGDFREPEVF DHIMAEVGDR
     QVDVVLSDMA PNTAGNSAID QPRMMYLCEL AVDFALATLP EGGALIMKVF QGEGTQELRK
     QMQADFSKIR SIKPGASRPR SKEMFWIAIK
 
 
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