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P75864 (RLMKL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal RNA large subunit methyltransferase K/L

Including the following 2 domains:

  1. 23S rRNA m2G2445 methyltransferase
    EC=2.1.1.173
    Alternative name(s):
    rRNA (guanine-N(2)-)-methyltransferase RlmL
  2. 23S rRNA m7G2069 methyltransferase
    EC=2.1.1.264
    Alternative name(s):
    rRNA (guanine-N(7)-)-methyltransferase RlmK
Gene names
Name:rlmL
Synonyms:rlmK, rlmKL, ycbY
Ordered Locus Names:b0948, JW0931
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits. Ref.4 Ref.6 Ref.7

Catalytic activity

S-adenosyl-L-methionine + guanine(2445) in 23S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(2445) in 23S rRNA. Ref.4 Ref.6 Ref.7

S-adenosyl-L-methionine + guanine(2069) in 23S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(2069) in 23S rRNA. Ref.4 Ref.6 Ref.7

Enzyme regulation

The N-terminal RlmL activity is enhanced by the C-terminal RlmK activity. Ref.6

Subunit structure

Monomer. Ref.7

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01858.

Domain

Consists of a N-terminal RlmL domain and a C-terminal RlmK domain, linked by a highly flexible loop. Ref.6 Ref.7

Sequence similarities

Belongs to the methyltransferase superfamily. RlmKL family.

Contains 1 THUMP domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

typAP321323EBI-547718,EBI-562154

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 702702Ribosomal RNA large subunit methyltransferase K/L HAMAP-Rule MF_01858
PRO_0000140473

Regions

Domain43 – 154112THUMP
Region1 – 397397RlmL HAMAP-Rule MF_01858
Region398 – 702305RlmK HAMAP-Rule MF_01858

Experimental info

Mutagenesis1951D → A: Does not affect methyltransferase activity. Ref.6
Mutagenesis3091N → A: Impairs m2G2445 formation, but does not affect m7G2069 formation. Ref.6
Mutagenesis3971N → A: Impairs m2G2445 formation, but does not affect m7G2069 formation. Ref.6
Mutagenesis5301R → A: Does not affect methyltransferase activity. Ref.6
Mutagenesis5681D → A: Impairs m7G2069 formation, but does not affect m2G2445 formation. Ref.6
Mutagenesis5971D → A: Does not affect methyltransferase activity. Ref.6

Secondary structure

................................................................................................................ 702
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P75864 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 9EF24AD7A32AC429

FASTA70278,854
        10         20         30         40         50         60 
MNSLFASTAR GLEELLKTEL ENLGAVECQV VQGGVHFKGD TRLVYQSLMW SRLASRIMLP 

        70         80         90        100        110        120 
LGECKVYSDL DLYLGVQAIN WTEMFNPGAT FAVHFSGLND TIRNSQYGAM KVKDAIVDAF 

       130        140        150        160        170        180 
TRKNLPRPNV DRDAPDIRVN VWLHKETASI ALDLSGDGLH LRGYRDRAGI APIKETLAAA 

       190        200        210        220        230        240 
IVMRSGWQPG TPLLDPMCGS GTLLIEAAML ATDRAPGLHR GRWGFSGWAQ HDEAIWQEVK 

       250        260        270        280        290        300 
AEAQTRARKG LAEYSSHFYG SDSDARVIQR ARTNARLAGI GELITFEVKD VAQLTNPLPK 

       310        320        330        340        350        360 
GPYGTVLSNP PYGERLDSEP ALIALHSLLG RIMKNQFGGW NLSLFSASPD LLSCLQLRAD 

       370        380        390        400        410        420 
KQYKAKNGPL DCVQKNYHVA ESTPDSKPAM VAEDYTNRLR KNLKKFEKWA RQEGIECYRL 

       430        440        450        460        470        480 
YDADLPEYNV AVDRYADWVV VQEYAPPKTI DAHKARQRLF DIIAATISVL GIAPNKLVLK 

       490        500        510        520        530        540 
TRERQKGKNQ YQKLGEKGEF LEVTEYNAHL WVNLTDYLDT GLFLDHRIAR RMLGQMSKGK 

       550        560        570        580        590        600 
DFLNLFSYTG SATVHAGLGG ARSTTTVDMS RTYLEWAERN LRLNGLTGRA HRLIQADCLA 

       610        620        630        640        650        660 
WLREANEQFD LIFIDPPTFS NSKRMEDAFD VQRDHLALMK DLKRLLRAGG TIMFSNNKRG 

       670        680        690        700 
FRMDLDGLAK LGLKAQEITQ KTLSQDFARN RQIHNCWLIT AA 

« Hide

References

« Hide 'large scale' references
[1]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Identification of Escherichia coli m2G methyltransferases: I. the ycbY gene encodes a methyltransferase specific for G2445 of the 23 S rRNA."
Lesnyak D.V., Sergiev P.V., Bogdanov A.A., Dontsova O.A.
J. Mol. Biol. 364:20-25(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[5]"Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m(2)G2445 methyltransferase RlmL from Escherichia coli."
Wang K.T., Ma L., Nan J., Su X.D., Li L.
Acta Crystallogr. F 66:1484-1486(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[6]"Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity."
Kimura S., Ikeuchi Y., Kitahara K., Sakaguchi Y., Suzuki T., Suzuki T.
Nucleic Acids Res. 40:4071-4085(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DOMAIN, MUTAGENESIS OF ASP-195; ASN-309; ASN-397; ARG-530; ASP-568 AND ASP-597.
[7]"Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA."
Wang K.T., Desmolaize B., Nan J., Zhang X.W., Li L.F., Douthwaite S., Su X.D.
Nucleic Acids Res. 40:5138-5148(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74034.1.
AP009048 Genomic DNA. Translation: BAA35703.1.
PIRC64835.
RefSeqNP_415468.1. NC_000913.3.
YP_489220.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3V8VX-ray2.60A/B1-702[»]
3V97X-ray2.20A/B1-702[»]
ProteinModelPortalP75864.
SMRP75864. Positions 1-702.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11486N.
IntActP75864. 48 interactions.
MINTMINT-1268879.
STRING511145.b0948.

Proteomic databases

PaxDbP75864.
PRIDEP75864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74034; AAC74034; b0948.
BAA35703; BAA35703; BAA35703.
GeneID12931031.
945564.
KEGGecj:Y75_p0920.
eco:b0948.
PATRIC32117115. VBIEscCol129921_0982.

Organism-specific databases

EchoBASEEB3481.
EcoGeneEG13717. rlmL.

Phylogenomic databases

eggNOGCOG0116.
HOGENOMHOG000218371.
KOK12297.
OMANKRGFKM.
OrthoDBEOG6HJ238.
PhylomeDBP75864.
ProtClustDBPRK11783.

Enzyme and pathway databases

BioCycEcoCyc:G6488-MONOMER.
ECOL316407:JW0931-MONOMER.
MetaCyc:G6488-MONOMER.

Gene expression databases

GenevestigatorP75864.

Family and domain databases

HAMAPMF_01858. 23SrRNA_methyltr_KL.
InterProIPR017244. 23SrRNA_methyltr_KL.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR000241. RNA_methylase_dom.
IPR019614. SAM-dep_methyl-trfase.
IPR004114. THUMP.
[Graphical view]
PfamPF10672. Methyltrans_SAM. 1 hit.
PF02926. THUMP. 1 hit.
PF01170. UPF0020. 1 hit.
[Graphical view]
PIRSFPIRSF037618. RNA_Mtase_bacteria_prd. 1 hit.
PRINTSPR00507. N12N6MTFRASE.
SMARTSM00981. THUMP. 1 hit.
[Graphical view]
PROSITEPS51165. THUMP. 1 hit.
PS01261. UPF0020. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP75864.

Entry information

Entry nameRLMKL_ECOLI
AccessionPrimary (citable) accession number: P75864
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene