CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005449
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA-specific 2-thiouridylase MnmA 
Protein Synonyms/Alias
  
Gene Name
 mnmA 
Gene Synonyms/Alias
 asuE; trmU; ycfB; b1133; JW1119 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
104NPDILCNKEIKFKAFacetylation[1]
107ILCNKEIKFKAFLEFacetylation[1]
149LRGLDSNKDQSYFLYacetylation[1, 2]
175FPVGELEKPQVRKIAacetylation[1]
252GLGIGGTKEGTEEPWacetylation[1]
264EPWYVVDKDVENNILacetylation[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]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111
Functional Description
 Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs. 
Sequence Annotation
 NP_BIND 11 18 ATP.
 REGION 97 99 Interaction with target base in tRNA.
 REGION 149 151 Interaction with tRNA.
 REGION 243 252 Interaction with tRNA.
 REGION 311 312 Interaction with tRNA.
 ACT_SITE 102 102 Nucleophile.
 ACT_SITE 199 199 Cysteine persulfide intermediate.
 BINDING 37 37 ATP; via amide nitrogen and carbonyl
 BINDING 127 127 ATP; via amide nitrogen.
 DISULFID 102 199 Alternate.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; Nucleotide-binding; Reference proteome; RNA-binding; Transferase; tRNA processing; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 368 AA 
Protein Sequence
MSETAKKVIV GMSGGVDSSV SAWLLQQQGY QVEGLFMKNW EEDDGEEYCT AAADLADAQA 60
VCDKLGIELH TVNFAAEYWD NVFELFLAEY KAGRTPNPDI LCNKEIKFKA FLEFAAEDLG 120
ADYIATGHYV RRADVDGKSR LLRGLDSNKD QSYFLYTLSH EQIAQSLFPV GELEKPQVRK 180
IAEDLGLVTA KKKDSTGICF IGERKFREFL GRYLPAQPGK IITVDGDEIG EHQGLMYHTL 240
GQRKGLGIGG TKEGTEEPWY VVDKDVENNI LVVAQGHEHP RLMSVGLIAQ QLHWVDREPF 300
TGTMRCTVKT RYRQTDIPCT VKALDDDRIE VIFDEPVAAV TPGQSAVFYN GEVCLGGGII 360
EQRLPLPV 368 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016783; F:sulfurtransferase activity; IDA:EcoCyc.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0002143; P:tRNA wobble position uridine thiolation; IDA:EcoCyc. 
Interpro
 IPR023382; Adenine_a_hdrlase_dom.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR004506; tRNA-specific_2-thiouridylase. 
Pfam
 PF03054; tRNA_Me_trans 
SMART
  
PROSITE
  
PRINTS