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Protein

Ribosomal RNA large subunit methyltransferase E

Gene

rlmE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(2552) in 23S rRNA.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=0.8 µM for 23S rRNA within 50S ribosomal subunits1 Publication
  2. KM=3.7 µM for S-adenosyl-L-methionine1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei63S-adenosyl-L-methionine; via amide nitrogen1 Publication1
    Binding sitei65S-adenosyl-L-methionine; via amide nitrogen1 Publication1
    Binding sitei83S-adenosyl-L-methionine1 Publication1
    Binding sitei99S-adenosyl-L-methionine1 Publication1
    Binding sitei124S-adenosyl-L-methionine1 Publication1
    Active sitei164Proton acceptor1 Publication1

    GO - Molecular functioni

    • rRNA (uridine-2'-O-)-methyltransferase activity Source: EcoCyc

    GO - Biological processi

    • enzyme-directed rRNA 2'-O-methylation Source: EcoCyc
    • ribosomal large subunit assembly Source: EcoCyc

    Keywordsi

    Molecular functionMethyltransferase, Transferase
    Biological processrRNA processing, Stress response
    LigandS-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11507-MONOMER
    MetaCyc:EG11507-MONOMER
    SABIO-RKiP0C0R7

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal RNA large subunit methyltransferase E (EC:2.1.1.166)
    Alternative name(s):
    23S rRNA Um2552 methyltransferase
    Cell division protein FtsJ
    rRNA (uridine-2'-O-)-methyltransferase
    Gene namesi
    Name:rlmE
    Synonyms:ftsJ, mrsF, rrmJ
    Ordered Locus Names:b3179, JW3146
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11507 rlmE

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show a dramatically altered ribosome profile, a severe growth disadvantage, and a temperature-sensitive phenotype. These effects are overcome by overexpressing either of 2 small GTPases, ObgE/CgtA or EngA.2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi20D → A: 2-fold decrease in activity. Increase in Km for 50S subunit. 1 Publication1
    Mutagenesisi22Y → A: No change in activity. 1 Publication1
    Mutagenesisi32R → A: 4-fold decrease in activity and increase in Km for 50S subunit; when associated with A-34. 1 Publication1
    Mutagenesisi34R → A: 4-fold decrease in activity and increase in Km for 50S subunit; when associated with A-32. 1 Publication1
    Mutagenesisi38K → A: Loss of activity. Almost no change in S-adenosyl-L-methionine binding. 1 Publication1
    Mutagenesisi83D → A: 5-fold decrease in activity. Increase in Km for 50S subunit and for S-adenosyl-L-methionine. Loss of S-adenosyl-L-methionine binding. 1 Publication1
    Mutagenesisi124D → A: Loss of activity. Loss of S-adenosyl-L-methionine binding. 1 Publication1
    Mutagenesisi136D → N: 2-fold decrease in activity. 1 Publication1
    Mutagenesisi164K → A: Loss of activity. No change in S-adenosyl-L-methionine binding. 1 Publication1
    Mutagenesisi189K → A: 9-fold decrease in activity. 1 Publication1
    Mutagenesisi194R → A: No change in activity. Increase in Km for 50S subunit. 1 Publication1
    Mutagenesisi197S → A: No change in activity. Increase in Km for 50S subunit. 1 Publication1
    Mutagenesisi199E → A: 16-fold decrease in activity. No change in S-adenosyl-L-methionine binding. 1 Publication1
    Mutagenesisi201Y → A: 5-fold decrease in activity. Almost no change in S-adenosyl-L-methionine binding. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001554971 – 209Ribosomal RNA large subunit methyltransferase EAdd BLAST209

    Proteomic databases

    PaxDbiP0C0R7
    PRIDEiP0C0R7

    Expressioni

    Inductioni

    By heat shock.

    Interactioni

    Protein-protein interaction databases

    BioGridi4262423, 299 interactors
    DIPiDIP-47902N
    IntActiP0C0R7, 22 interactors
    STRINGi316385.ECDH10B_3353

    Structurei

    Secondary structure

    1209
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi34 – 46Combined sources13
    Beta strandi54 – 59Combined sources6
    Helixi64 – 73Combined sources10
    Beta strandi78 – 85Combined sources8
    Beta strandi93 – 98Combined sources6
    Helixi103 – 113Combined sources11
    Beta strandi118 – 123Combined sources6
    Helixi133 – 154Combined sources22
    Beta strandi155 – 168Combined sources14
    Helixi171 – 181Combined sources11
    Beta strandi182 – 188Combined sources7
    Beta strandi199 – 207Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EIZX-ray1.70A30-209[»]
    1EJ0X-ray1.50A30-209[»]
    ProteinModelPortaliP0C0R7
    SMRiP0C0R7
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C0R7

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105F7M Bacteria
    COG0293 LUCA
    HOGENOMiHOG000162367
    InParanoidiP0C0R7
    KOiK02427
    OMAiHRQTDHL
    PhylomeDBiP0C0R7

    Family and domain databases

    HAMAPiMF_01547 RNA_methyltr_E, 1 hit
    InterProiView protein in InterPro
    IPR015507 rRNA-MeTfrase_E
    IPR002877 rRNA_MeTrfase_FtsJ_dom
    IPR004512 rRNA_MeTrfase_gammaproteobac
    IPR029063 SAM-dependent_MTases
    PfamiView protein in Pfam
    PF01728 FtsJ, 1 hit
    PIRSFiPIRSF005461 23S_rRNA_mtase, 1 hit
    SUPFAMiSSF53335 SSF53335, 1 hit
    TIGRFAMsiTIGR00438 rrmJ, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P0C0R7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTGKKRSASS SRWLQEHFSD KYVQQAQKKG LRSRAWFKLD EIQQSDKLFK
    60 70 80 90 100
    PGMTVVDLGA APGGWSQYVV TQIGGKGRII ACDLLPMDPI VGVDFLQGDF
    110 120 130 140 150
    RDELVMKALL ERVGDSKVQV VMSDMAPNMS GTPAVDIPRA MYLVELALEM
    160 170 180 190 200
    CRDVLAPGGS FVVKVFQGEG FDEYLREIRS LFTKVKVRKP DSSRARSREV

    YIVATGRKP
    Length:209
    Mass (Da):23,335
    Last modified:December 6, 2005 - v1
    Checksum:iB83C3A7DFA8AC78F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M83138 Genomic DNA Translation: AAA23812.1
    U01376 Genomic DNA Translation: AAA97507.1
    U18997 Genomic DNA Translation: AAA57980.1
    U00096 Genomic DNA Translation: AAC76211.1
    AP009048 Genomic DNA Translation: BAE77223.1
    PIRiS35108
    RefSeqiNP_417646.1, NC_000913.3
    WP_000145975.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC76211; AAC76211; b3179
    BAE77223; BAE77223; BAE77223
    GeneIDi947689
    KEGGiecj:JW3146
    eco:b3179
    PATRICifig|1411691.4.peg.3553

    Similar proteinsi

    Entry informationi

    Entry nameiRLME_ECOLI
    AccessioniPrimary (citable) accession number: P0C0R7
    Secondary accession number(s): P28692, Q2M933
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: March 28, 2018
    This is version 104 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health