Latest update: September 24, 2018


ProGT103 (EarP)

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

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., Fürst, M., Wuichet, K., Gödeke, J., Starosta, A.L., Chen, J.M., Søgaard-Andersen, L., Rohr, J., Wilson, D.N.& Häussler, 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., Fürst, M., Wuichet, K., Gödeke, J., Starosta, A.L., Chen, J.M., Søgaard-Andersen, L., Rohr, J., Wilson, D.N.& Häussler, 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 Häussler, 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.