Latest update: September 24, 2018


ProGT79 (BAHTCr)

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ProGT ID ProGT79 (BAHTCr)
Organism Information
Organism NameCitrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280)
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Enterobacteriaceae
Order: Enterobacteriales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)637910
Genome Information
Gene BankFN543503
EMBLFN543503
Gene Information
Gene NameROD_p1111
NCBI Reference SequenceFN543503
Protein information
Protein NameBAHTCr 
UniProtKB/ SwissProt IDD2TV87
NCBI Ref SeqWP_012908907.1
UniProtKB Sequence>tr|D2TV87|D2TV87_CITRI Putative adhesin glycosyltransferase OS=Citrobacter rodentium (strain ICC168) GN=ROD_p1111 PE=4 SV=1 MQKSLATFFISPPEIPTQHGPDNILYDFNDGARVLLPEGKWHVRLLDADSGNILFCCDIN NGWVTSSKKYFVRFRIQVFRQGEDSPLLDETLNLTDRDVLISFPTGTLGDLLGWFPYAER FQSLHQCRLECTMAQDIIDLLAPQYPQICFSTPEKPRTTEPYATYRVGLYFGGDTNNQPV DFRQVGFHRSAGYILGVDPREAPVRLNLSAPCTIREPYVCIATQSTCQAKYWNNGTGWSE VVAHLKSLGYRVLCIDREAHYGQGFVWNHIPWGAEDFTGSFPLQERVNLLRHASFFIGLA SGLSWLAWATGIPVVLISGFSLPDSEFYTPWRVFNSHGCNGCWDDTSLNFDHKDFLWCPR HKNTDRQFECTRLITGTQVNGVISRLHASLMKQGDKACLTKGTNNEQGL
EMBL CDSCBG91773.1
Sequence length409 AA
Additional Information1) BAHTCr, heptosyltransferases able complement AAH (E. coli) in restoring AIDA-I glycosylation and bacterial adhesion to HeLa cells.
2) BAHTCr is involved in a transfer of heptose to CARC autotransporter which is very critical for C. rodentium colonization in mice colon.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
CAZY FamilyGTNC
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeNucleotide activated sugars
Donor SpecificityADP-Heptose
Glycan Information
Glycan transferredMonosaccharide (Heptose) 
Method of Glycan IndentificationECL glycoprotein detection kit
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name AIDA-I (CARC)
ProGPdb ID ProGP201
Acceptor Substrate name TibA
ProGPdb ID ProGP176
Litrature
Year Of Validation2014 
Reference Lu, Q., Yao, Q., Xu, Y., Li, L., Li, S., Liu, Y., Gao, W., Niu, M., Sharon, M., Ben-Nissan, G. & Zamyatina, A. (2014). An iron-containing dodecameric heptosyltransferase family modifies bacterial autotransporters in pathogenesis. Cell host & microbe, 16(3), 351-363.

Authors Lu, Q., Yao, Q., Xu, Y., Li, L., Li, S., Liu, Y., Gao, W., Niu, M., Sharon, M., Ben-Nissan, G. & Zamyatina, A.
Research groups1 National Institute of Biological Sciences, Beijing 102206, China.National Institute of Biological Sciences, Beijing 102206, China. 2 College of Biological Sciences, China Agricultural University, Beijing 100094, China. 3 Institute of Analytical Chemistry & Synthetic and Functional Biomolecules Center. 4 College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China. 5 Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel. 6 Department of Chemistry, University of Natural Resources and Life Sciences, A-1190 Vienna, Austria. 7 National Institute of Biological Sciences, Beijing 102206, China. 8 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. 9 National Institute of Biological Sciences, Beijing, Collaborative Innovation Center for Cancer Medicine, Beijing 102206, China.
Corresponding Author Zamyatina, A.
Contacts1 National Institute of Biological Sciences, Beijing 102206, China. 2 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, 3 China 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., ... & Shao, F. (2014). A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family. Elife, 3, e03714.

Authors Yao, Q., Lu, Q., Wan, X., Song, F., Xu, Y., Hu, M., ... & Shao, F.
Research groups1 Dr Feng Shaos Laboratory, National Institute of Biological Sciences, Beijing, China. 2 Dr Niu Huangs Laboratory, National Institute of Biological Sciences, Beijing, China. 3 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. 4 Institute of Analytic Chemistry, College of Chemistry and Molecular Engineering, Peking University, Beijing, China. 5 Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Corresponding Author Shao, F.
ContactsDr Feng Shaos Laboratory, National Institute of Biological Sciences, Beijing, China