Latest update: September 24, 2018


ProGT11 (TibC)

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

ProGT ID ProGT11 (TibC)
Organism Information
Organism NameEscherichia coli ETEC
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Enterobacteriaceae
Order: Enterobacteriales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)316401
Genome Information
Gene BankAF131891
EMBLAF131891
Gene Information
Gene NametibC
Protein information
Protein NameTibC 
UniProtKB/ SwissProt IDQ9S4K6
NCBI Ref SeqWP_000105682.1
UniProtKB Sequence>sp|Q9S4K6|TIBC_ECOH1 Glycosyltransferase TibC OS=Escherichia coli O78:H11 (strain H10407 / ETEC) GN=tibC PE=1 SV=1 MSTLKNTFFITPPDTPTQAGPENIFYDFNDGARVLLPEGKWHVRLLDADSENILFCCDVD KGWVTSSKKYFVRFRIQVFRQGEETPLLDETLKLKDRPVLISFPTGTLGDLLGWFPYAER FQSLHKCRLECTMSQDIIDLLAPQYPQIQFSTPDKPRTVAPYATYRVGLYFGGDTNNQPV DFRKVGFHRSAGYILGVDPREAPVRLDLSAPRVIQEPYVCIATQSTCQAKYWNNGTGWSE VIAHLKSLGYRVMCIDRDAHYGQGFVWNHIPWGAEDFTGKLPLQERVNLLRHASFFIGLP SGLSWLAWATRIPVVLISGFSLPNSEFYTPWRVFNSHGCYGCWDDTSLNFDHHDFLWCPR HKNTDRQFECTRLITGAQVNGVINKLHRSLTEQGVEATLKKGVSNE
EMBL CDSAAD46996.1
Sequence length406 AA
Subcellular LocationCytoplasm
Function in Native Organism 1) TibC is the protein transfer the heptose sugar to the protein TibA.
PDB ID 4RAP 4RB4
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
CAZY FamilyGTNC
EC Number (BRENDA)2.4.99
Mechanism of Glycan TransferSequential
Acceptor specificity Sequon_1NGGKTTATTVNSSGSQNVG
Donor TypeNucleotide activated sugars
Donor SpecificityADP-Heptose
Glycan Information
Glycan transferredMonosaccharide (Heptose) 
Method of Glycan IndentificationDIG glycan detection
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name TibA
ProGPdb ID ProGP176
Acceptor Substrate name AIDA-I
ProGPdb ID ProGP201
Litrature
Year Of Validation2002 
Reference Moormann, C., Benz, I., & Schmidt, M. A. (2002). Functional substitution of the TibC protein of enterotoxigenic Escherichia coli strains for the autotransporter adhesin heptosyltransferase of the AIDA system. Infection and immunity, 70(5), 2264-2270.

Authors Moormann, C., Benz, I., & Schmidt, M. A.
Research groupsInstitute of Infectiology, Center for Molecular Biology of Inflammation, West of Wilhelms-University of Münster, D-48149 Münster, Germany.
Corresponding Author Schmidt, M. A.
ContactsInstitute of Infectiology, Center for Molecular Biology of Inflammation, West of Wilhelms-University of Münster, D-48149 Münster, Germany.
Reference Charbonneau, M.È., Côté, J.P., Haurat, M.F., Reiz, B., Crépin, S., Berthiaume, F., Dozois, C.M., Feldman, M.F. & Mourez, M. (2012). A structural motif is the recognition site for a new family of bacterial protein O?glycosyltransferases. Molecular microbiology, 83(5), 894-907.

Authors Charbonneau, M.È., Côté, J.P., Haurat, M.F., Reiz, B., Crépin, S., Berthiaume, F., Dozois, C.M., Feldman, M.F. & Mourez, M.
Research groupsCanada Research Chair on Bacterial Animal Diseases, University of Montreal, Faculty of Veterinary Medicine St-Hyacinthe, 3200 Sicotte, St-Hyacinthe, Quebec, Canada.
Corresponding Author Mourez, M.
ContactsCanada Research Chair on Bacterial Animal Diseases, University of Montreal, Faculty of Veterinary Medicine St-Hyacinthe, 3200 Sicotte, St-Hyacinthe, Quebec, Canada.