CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010350
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA sulfurtransferase 
Protein Synonyms/Alias
 Sulfur carrier protein ThiS sulfurtransferase; Thiamine biosynthesis protein ThiI; tRNA 4-thiouridine synthase 
Gene Name
 thiI 
Gene Synonyms/Alias
 yajK; b0423; JW0413 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
14LFPEITIKSQSVRLRacetylation[1]
24SVRLRFIKILTGNIRacetylation[1]
35GNIRNVLKHYDETLAacetylation[1]
265GQMGVILKRMMVRAAacetylation[1]
321RPLISYDKEHIINLAacetylation[1]
422SIDEQEDKPLKVEGIacetylation[1]
425EQEDKPLKVEGIDVVacetylation[1]
438VVSLPFYKLSTKFGDacetylation[1]
442PFYKLSTKFGDLDQNacetylation[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
 Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. 
Sequence Annotation
 DOMAIN 61 165 THUMP.
 DOMAIN 404 482 Rhodanese.
 NP_BIND 183 184 ATP (By similarity).
 ACT_SITE 456 456 Cysteine persulfide intermediate.
 BINDING 265 265 ATP (By similarity).
 BINDING 287 287 ATP; via amide nitrogen (By similarity).
 BINDING 296 296 ATP (By similarity).
 DISULFID 344 456 Redox-active.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; Nucleotide-binding; Redox-active center; Reference proteome; RNA-binding; Thiamine biosynthesis; Transferase; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 482 AA 
Protein Sequence
MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR 60
LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALVQYRD QLEGKTFCVR VKRRGKHDFS 120
SIDVERYVGG GLNQHIESAR VKLTNPDVTV HLEVEDDRLL LIKGRYEGIG GFPIGTQEDV 180
LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGAAHEIGV RQVAHYLWNR FGSSHRVRFV 240
AINFEPVVGE ILEKIDDGQM GVILKRMMVR AASKVAERYG VQALVTGEAL GQVSSQTLTN 300
LRLIDNVSDT LILRPLISYD KEHIINLARQ IGTEDFARTM PEYCGVISKS PTVKAVKSKI 360
EAEEEKFDFS ILDKVVEEAN NVDIREIAQQ TEQEVVEVET VNGFGPNDVI LDIRSIDEQE 420
DKPLKVEGID VVSLPFYKLS TKFGDLDQNK TWLLWCERGV MSRLQALYLR EQGFNNVKVY 480
RP 482 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0016783; F:sulfurtransferase activity; IEA:HAMAP.
 GO:0000049; F:tRNA binding; IEA:HAMAP.
 GO:0009228; P:thiamine biosynthetic process; IEA:HAMAP.
 GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0052837; P:thiazole biosynthetic process; IEA:InterPro.
 GO:0034227; P:tRNA thio-modification; IEA:HAMAP. 
Interpro
 IPR001763; Rhodanese-like_dom.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR026340; Thiazole_biosynth_dom.
 IPR003720; ThiI.
 IPR020536; ThiI_C_dom.
 IPR004114; THUMP. 
Pfam
 PF02568; ThiI
 PF02926; THUMP 
SMART
 SM00981; THUMP 
PROSITE
 PS50206; RHODANESE_3
 PS51165; THUMP 
PRINTS