CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002418
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosomal RNA small subunit methyltransferase A 
Protein Synonyms/Alias
 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase; 16S rRNA dimethyladenosine transferase; 16S rRNA dimethylase; High level kasugamycin resistance protein KsgA; Kasugamycin dimethyltransferase; S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 
Gene Name
 rsmA 
Gene Synonyms/Alias
 ksgA; b0051; JW0050 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
205ATMPHPVKDVRVLSRacetylation[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 dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Has also a DNA glycosylase/AP lyase activity that removes C mispaired with oxidized T from DNA, and may play a role in protection of DNA against oxidative stress. 
Sequence Annotation
 BINDING 18 18 S-adenosyl-L-methionine; via carbonyl
 BINDING 20 20 S-adenosyl-L-methionine; via amide
 BINDING 45 45 S-adenosyl-L-methionine; via carbonyl
 BINDING 66 66 S-adenosyl-L-methionine (By similarity).
 BINDING 91 91 S-adenosyl-L-methionine (By similarity).
 BINDING 113 113 S-adenosyl-L-methionine (By similarity).  
Keyword
 3D-structure; Antibiotic resistance; Complete proteome; Cytoplasm; Direct protein sequencing; Methyltransferase; Reference proteome; RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 273 AA 
Protein Sequence
MNNRVHQGHL ARKRFGQNFL NDQFVIDSIV SAINPQKGQA MVEIGPGLAA LTEPVGERLD 60
QLTVIELDRD LAARLQTHPF LGPKLTIYQQ DAMTFNFGEL AEKMGQPLRV FGNLPYNIST 120
PLMFHLFSYT DAIADMHFML QKEVVNRLVA GPNSKAYGRL SVMAQYYCNV IPVLEVPPSA 180
FTPPPKVDSA VVRLVPHATM PHPVKDVRVL SRITTEAFNQ RRKTIRNSLG NLFSVEVLTG 240
MGIDPAMRAE NISVAQYCQM ANYLAENAPL QES 273 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:EC.
 GO:0003690; F:double-stranded DNA binding; IDA:EcoCyc.
 GO:0003729; F:mRNA binding; IDA:EcoCyc.
 GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IDA:EcoCyc.
 GO:0019843; F:rRNA binding; IDA:EcoCyc.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0000028; P:ribosomal small subunit assembly; IMP:EcoCyc.
 GO:0070475; P:rRNA base methylation; IMP:EcoCyc. 
Interpro
 IPR023165; rRNA_Ade_diMease-like.
 IPR020596; rRNA_Ade_Mease_Trfase_CS.
 IPR001737; rRNA_Ade_methylase_transferase.
 IPR020598; rRNA_Ade_methylase_Trfase_N.
 IPR011530; rRNA_adenine_dimethylase. 
Pfam
 PF00398; RrnaAD 
SMART
 SM00650; rADc 
PROSITE
 PS01131; RRNA_A_DIMETH 
PRINTS