Latest update: September 24, 2018


ProGT106 (SseK3)

Home -> ProGTdb -> Search ProGT_Main -> Display data

ProGT ID ProGT106 (SseK3)
Organism Information
Organism NameSalmonella typhimurium (strain SL1344)
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Enterobacteriaceae
Order: Enterobacteriales
Class: Gammaproteobacteria
Phylum: Proteobacteria
Taxonomic ID (NCBI)216597
Genome Information
Gene BankFQ312003
EMBLFQ312003
Gene Information
Gene NamesseK3
Protein information
Protein NameSseK3 
UniProtKB/ SwissProt IDA0A0H3NMP8
NCBI Ref SeqWP_000492926.1
UniProtKB Sequence>tr|A0A0H3NMP8|A0A0H3NMP8_SALTS Type III secretion system effector protein OS=Salmonella typhimurium (strain SL1344) GN=sseK3 PE=4 SV=1 MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRF GENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVI YNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSS HDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYL PDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYF NCSIRHNYEEFCNFIEFKHEHIFMDTSSLTISSWR
EMBL CDSCBW18025.1
Sequence length335 AA
Function in Native Organism 1) The SseK3 translocates into host cells, targeting innate immune responses, including NF-?B activation.
Additional Information1) SseK3 is the first structure of a retaining arginine glycosyltransferase bound to a hydrolyzed form of its donor substrate.
2) SseK3-mediated inhibition of TNF-alpha-induced NF-?B activation, directly correlating enzymatic activity to virulence function.
PDB ID 6EYR 6EYT 6CGI
Glycosyltransferase Information
Glycosylation TypeN- (Arg) linked  
EC Number (BRENDA)2.4.99.18
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificityUDP-GlcNAc
Glycan Information
Glycan transferredMonosaccharide (GlcNAc) 
Acceptor Subtrate Information
Acceptor Substrate name TRADD
Litrature
Year Of Validation2015 
Reference Esposito, D., Günster, R. A., Martino, L., El Omari, K., Wagner, A., Thurston, T. L., & Rittinger, K. (2018). Structural basis for the glycosyltransferase activity of the Salmonella effector SseK3. Journal of Biological Chemistry, jbc-RA118.

Authors Esposito, D., Günster, R. A., Martino, L., El Omari, K., Wagner, A., Thurston, T. L., & Rittinger, K.
Research groups1 Molecular Structure of Cell Signalling Laboratory, Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom. 2 Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, United Kingdom. 3 Diamond Light Source, Harwell Science and Innovation Campus, Chilton, Didcot OX11 0DE, United Kingdom. 4 Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, United Kingdom. 5 Molecular Structure of Cell Signalling Laboratory, Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom.
Corresponding Author Rittinger, K.
Contacts1 Molecular Structure of Cell Signalling Laboratory, Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom. 2 Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, United Kingdom. 3 Diamond Light Source, Harwell Science and Innovation Campus, Chilton, Didcot OX11 0DE, United Kingdom. 4 Section of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, United Kingdom. 5 Molecular Structure of Cell Signalling Laboratory, Francis Crick Institute, 1 Midland Road, London NW1 1AT, United Kingdom.