Latest update: September 24, 2018


ProGT118 (EarP)

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ProGT ID ProGT118 (EarP)
Organism Information
Organism NamePseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Pseudomonadaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)160488
Genome Information
Gene BankAE015451
EMBLAE015451
Gene Information
Gene NameearP
NCBI Gene ID1043242
Protein information
Protein NameEF-P arginine 32 rhamnosyl-transferase 
UniProtKB/ SwissProt IDQ88LS1
NCBI Ref SeqWP_010952888.1
UniProtKB Sequence>tr|Q88LS1|Q88LS1_PSEPK EF-P arginine 32 rhamnosyl-transferase OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440) OX=160488 GN=earP PE=1 SV=1 MKATWDIFCSVVDNYGDIGVTWRLARQLVAEHGLAVRLWVDDLNAFTPMCPGADATAAQQ WQHGVDVRHWPAAWLPVAPADVVIGAFACQLPAAYVEAMRARPQPPLWLNLEYLSAEDWV EGCHGLPSPQPNGLRKVFFFPGFTDKTGGLLREGSLLARRDGFQQSAEARRAFLQGLGVD LVPGALLISLFAYENPQLGNWLDALATADQPCHLLVPQGRVVAGLSQWLGEGPLHVGDVR TRGALTVQVLPFVSQDDFDRLLWSCDFNAVRGEDSFVRAQWAGQPMLWHIYVQDENAHWE KLEAFLAHYRCGLSDDADAALLGLWRAWNMDFDMGQAWRAARQHWPELQQHARLWGARQA AQPDLATALVHFYRNSL
EMBL CDSAAN67476
Sequence length377 AA
String160488.PP_1857
Potential Application1) The structures of EarP in complex with substrates should provide valuable information for the structure-guided development of its inhibitors such as EarP-containing pathogens specific antibacterials.
Additional Information1) EarP is an EF-P arginine rhamnosyltransferase which is essential for post-translational activation.
2) EF-P and the corresponding rhamnosyltransferase EarP contributes to pathogenicity in Pseudomonas putida.
3) KOW-like EF-P N-domain is sufficient for EarP-mediated rhamnosylation.
PDB ID 5NV8
Glycosyltransferase Information
Glycosylation TypeN- (Arg) linked  
CAZY FamilyGT104
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificitydTDP-l-Rhamnose
Glycan Information
Glycan transferredMonosaccharide (Rha) 
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name EF-P
ProGPdb ID ProGP686
Litrature
Year Of Validation2017 
Reference Krafczyk, R., Macošek, J., Jagtap, P.K.A., Gast, D., Wunder, S., Mitra, P., Jha, A.K., Rohr, J., Hoffmann-Röder, A., Jung, K. & Hennig, J. (2017). Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P. MBio, 8(5), e01412-17.

Authors Krafczyk, R., Macošek, J., Jagtap, P.K.A., Gast, D., Wunder, S., Mitra, P., Jha, A.K., Rohr, J., Hoffmann-Röder, A., Jung, K. & Hennig, J.
Research groups1 Center for integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany. 2 Structural and Computational Biology Unit, EMBL Heidelberg, Heidelberg, Germany. 3 Center for integrated Protein Science Munich (CiPSM), Department of Chemistry, Ludwig-Maximilians-Universität München, Munich, Germany. 4 University of Kentucky College of Pharmacy, Lexington, Kentucky, USA. 5 Structural and Computational Biology Unit, EMBL Heidelberg, Heidelberg, Germany. 6 Center for integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany
Corresponding Author Hennig, J.
Contacts1 Center for integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany.