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ProGT103 (EarP)

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ProGT ID ProGT103 (EarP)
Organism Information
Organism NamePseudomonas aeruginosa PAO1
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Pseudomonadaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)208964
Genome Information
Gene BankAE004091
EMBLAE004091
Gene Information
Gene NamePA2852
NCBI Gene ID882634
Protein information
Protein NameEarP 
UniProtKB/ SwissProt IDQ9HZZ1
NCBI Ref SeqAAG06240.1
UniProtKB Sequence>tr|Q9HZZ1|Q9HZZ1_PSEAE Uncharacterized protein OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) GN=PA2852 PE=4 SV=1 MASWDIFCSVVDNYGDIGVTWRLARQLAAEHGQAVRLWVDEPQAFARICPRADPVAHVQC LDGVEVRAWGRPWAPVAAADVVIEAFACELPEAHRQAMRERKRPSLWLNLEYLSAEEWIG SCHALPSLQACGLSKYFFFPGFREPSGGLLREAGLLERRRRFQASVSAQDEFLASLGVRR KVGERLISLFAYENPALPGWLEQLRDARQPSLLLVPEGRVLADVADWLRVATLAVGDVHV RDALRVQVLPFMAQDDYDRLLWCCDLNAVRGEDSFVRAQWAGRPLLWHIYRQEEETHLAK LEAFLELYCAGLPADLAENLRTFWLAWNAGGGLAGAWEGLERQLPEWRREAQRWADEQGM RPDLAARLVQFYADWL
EMBL CDSAAG06240.1
Sequence length376 AA
Function in Native Organism 1) EarP and EF-P are essential for P. aeruginosa pathogenicity.
String208964.PA2852
Potential Application1) Inhibitors targeting EarP type glycosyltransferase helps in the development of specific antibiotics against pathogens.
Additional Information1) EarP is an EF-P arginine rhamnosyltransferase which is essential for post-translational activation.
2) Virulence factors, such as rhamnolipids and pyocyanin are important to P. aeruginosa PAO1 for colonization and invasion during infection.
Glycosyltransferase Information
Glycosylation TypeN- (Arg) linked  
CAZY FamilyGT104
EC Number (BRENDA)2.4.99.18
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificitydTDP-l-Rhamnose
Glycan Information
Glycan transferredMonosaccharide (Rha) 
Method of Glycan IndentificationLC-MS/MS
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name EF-P
ProGPdb ID ProGP495
Litrature
Year Of Validation2015 
Reference Lassak, J., Keilhauer, E.C., Frst, M., Wuichet, K., Gdeke, J., Starosta, A.L., Chen, J.M., Sgaard-Andersen, L., Rohr, J., Wilson, D.N.& Hussler, S. (2015). Arginine-rhamnosylation as new strategy to activate translation elongation factor P.Nature chemical biology,11(4), 266.

Authors Lassak, J., Keilhauer, E.C., Frst, M., Wuichet, K., Gdeke, J., Starosta, A.L., Chen, J.M., Sgaard-Andersen, L., Rohr, J., Wilson, D.N.& Hussler, S.
Research groups1 Center for Integrated Protein Science Munich, Ludwig-Maximilians-University of Munich, Munich, Germany. 2 Department of Biology I, Microbiology, Ludwig-Maximilians-University of Munich, Martinsried, Germany. 3 Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Martinsried, Germany. 4 Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. 5 Institute for Molecular Bacteriology, Twincore, Centre for Clinical and Experimental Infection Research, a joint venture of the Helmholtz Centre of Infection Research and the Hannover Medical School, Hannover, Germany. 7 Gene Center, Department for Biochemistry, Ludwig-Maximilians-University of Munich, Martinsried, Munich, Germany. 8 Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, Kentucky, USA. 9 Department of Molecular Bacteriology, Helmholtz Centre for Infection Research, Braunschweig, Germany.
Corresponding Author Hussler, S.
Contacts1 Center for Integrated Protein Science Munich, Ludwig-Maximilians-University Munich,, Munich, Germany. 2 Department of Biology I, Microbiology,Ludwig-Maximilians-University of Munich, Martinsried, Germany.