CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009709
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 23S rRNA (guanosine-2'-O-)-methyltransferase RlmB 
Protein Synonyms/Alias
 23S rRNA (guanosine2251 2'-O)-methyltransferase; 23S rRNA Gm2251 2'-O-methyltransferase 
Gene Name
 rlmB 
Gene Synonyms/Alias
 yjfH; b4180; JW4138 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
29FQEVFILKGREDKRLacetylation[1]
61NRQYLDEKSDGAVHQacetylation[1]
128VHAVIVPKDRSAQLNacetylation[1]
186DHTLYQSKMTGRLALacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 Specifically methylates the ribose of guanosine 2251 in 23S rRNA. 
Sequence Annotation
 BINDING 196 196 S-adenosyl-L-methionine; via carbonyl
 BINDING 216 216 S-adenosyl-L-methionine; via amide
 BINDING 225 225 S-adenosyl-L-methionine; via amide  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 243 AA 
Protein Sequence
MSEMIYGIHA VQALLERAPE RFQEVFILKG REDKRLLPLI HALESQGVVI QLANRQYLDE 60
KSDGAVHQGI IARVKPGRQY QENDLPDLIA SLDQPFLLIL DGVTDPHNLG ACLRSADAAG 120
VHAVIVPKDR SAQLNATAKK VACGAAESVP LIRVTNLART MRMLQEENIW IVGTAGEADH 180
TLYQSKMTGR LALVMGAEGE GMRRLTREHC DELISIPMAG SVSSLNVSVA TGICLFEAVR 240
QRS 243 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IMP:EcoCyc.
 GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IMP:EcoCyc. 
Interpro
 IPR024915; 23S_rRNA_MeTrfase_RlmB.
 IPR004441; rRNA_MeTrfase_TrmH.
 IPR001537; SpoU_MeTrfase.
 IPR013123; SpoU_subst-bd. 
Pfam
 PF00588; SpoU_methylase
 PF08032; SpoU_sub_bind 
SMART
 SM00967; SpoU_sub_bind 
PROSITE
  
PRINTS