ProGT8 (Aah)

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ProGT ID ProGT8 (Aah)
ProGT Pathway
Organism Information
Organism NameEscherichia coli K12
Clinical ImplicationNon-pathogenic
Classification Phylum : Proteobacteria
Class : GammaProteobacteria
Orders : Enterobacterales
Family : Enteerobacteriaceae
Genus : Escherichia
Species : coli
Taxonomic ID (NCBI)562
Genome Information
Gene BankGU810159
Gene Information
Gene Nameaah
NCBI Reference SequenceAJ304444.1
Protein information
Protein NameAah 
UniProtKB/ SwissProt IDQ93K96
Sequence length391 AA
Subcellular LocationCytoplasm
Function in Native Organism 1) Aah is a heptosyltransferase which transfers a heptose sugar to acceptor protein AIDA.
Additional Information1) AAH is the prototype of a new large family of bacterial protein O-glycosyltransferases that modify different substrates containing a structural motif of 19 amino acid consensus sequence.
2) Iron binding is required for AAH glycosyltransferase activity.
3) AAH and its paralogue AAH2 are heptosylating autotransporter AIDA-1 which is essential for pathogenesis and colonization in mice.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Acceptor specificity Sequon_1NGGKTTATTVNSSGSQNVG
Donor TypeADP-Heptose
Donor SpecificityNucleotide activated sugars
Glycan Information
Glycan transferredMonosaccharide (Heptose) 
Method of Glycan IndentificationGC MS, MS-MS (CID) and, MALDI-TOF
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name AIDA-I
ProGPdb ID ProGP201
Acceptor Substrate name Ag 43
ProGPdb ID ProGP249
Year Of Validation2001 
Reference Benz, I. and Schmidt, M.A., 2001. Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA?I adhesin. Molecular microbiology, 40(6), pp.1403-1413.

Corresponding AuthorInstitute of Infectiology - Center for Molecular Biology of Inflammation (ZMBE), University Hospital Münster, Germany
Reference Charbonneau, M.È., Girard, V., Nikolakakis, A., Campos, M., Berthiaume, F., Dumas, F., Lépine, F. and Mourez, M., 2007. O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence. Journal of bacteriology, 189(24), pp.8880-8889.

Corresponding AuthorUniversity of Montreal, Faculty of Veterinary Medicine, 3200 Sicotte, St.-Hyacinthe, Quebec J2S 7C6, Canada.
Reference Knudsen, S.K., Stensballe, A., Franzmann, M., Westergaard, U.B. and Otzen, D.E., 2008. Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation. Biochemical Journal, 412(3), pp.563-577.

Corresponding AuthorDepartment of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark.
Reference Charbonneau, M.È., Côté, J.P., Haurat, M.F., Reiz, B., Crépin, S., Berthiaume, F., Dozois, C.M., Feldman, M.F. and Mourez, M., 2012. A structural motif is the recognition site for a new family of bacterial protein O?glycosyltransferases. Molecular microbiology, 83(5), pp.894-907.

Corresponding AuthorCanada Research Chair on Bacterial Animal Diseases, University of Montreal, Faculty of Veterinary Medicine St-Hyacinthe, 3200 Sicotte, St-Hyacinthe, Quebec, Canada.
Reference Lu, Q., Yao, Q., Xu, Y., Li, L., Li, S., Liu, Y., Gao, W., Niu, M., Sharon, M., Ben-Nissan, G. and Zamyatina, A., 2014. An iron-containing dodecameric heptosyltransferase family modifies bacterial autotransporters in pathogenesis. Cell host & microbe, 16(3), pp.351-363.

Corresponding Author1 National Institute of Biological Sciences, Beijing 102206, China. 2 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. 3 National Institute of Biological Sciences, Beijing, Collaborative Innovation Center for Cancer Medicine, Beijing 102206, China.
Reference Yao, Q., Lu, Q., Wan, X., Song, F., Xu, Y., Hu, M., Zamyatina, A., Liu, X., Huang, N., Zhu, P. and Shao, F., 2014. A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family. Elife, 3, p.e03714.

Corresponding AuthorDr Feng Shao's Laboratory, National Institute of Biological Sciences, Beijing, China