Latest update: September 24, 2018


ProGT116 (EntS)

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ProGT ID ProGT116 (EntS)
ProGT Pathway
Organism Information
Organism NameEnterococcus faecalis TX0104
Clinical ImplicationPathogenic
DomainBacteria
PhylumFirmicutes
ClassificationFamily: Enterococcaceae
Order: Lactobacillales
Class: Bacilli
Phylum: Firmicutes
Taxonomic ID (NCBI)491074
Genome Information
Gene BankACGL01000031
EMBLACGL01000031
Gene Information
Gene NameHMPREF0348_0417
Protein information
Protein NameEntS 
UniProtKB/ SwissProt IDC0X1N2
NCBI Ref SeqEEI13070.1
UniProtKB Sequence>tr|C0X1N2|C0X1N2_ENTFL Glycosyltransferase, group 2 family protein OS=Enterococcus faecalis TX0104 GN=HMPREF0348_0417 PE=4 SV=1 MYSENFIANDWFNVEVFNKNKYTLTNQENKDVTELWLQILKGLKFPNELKETVSYSKNLK ELSLKTHAEVSVCIIAKNEQDSIRKCINSIYEFSDEIIFIDTGSIDSTKKIVKEIASEKV KIFDYTWQDDFSDARNYSIQKASKEWILIIDADEYVSSDELIKLRLLIDMLDRFKFKDSL RVSCAIYQLDNVITHGQSRLFRNNNKIKYYGLIHEELRNNKGLDPIFNVESEITFFHDGY KEILRKEKCERNIRLLAKMLEKEPDNVRWAYLYCRDSFSINSNIDFEKILLPFLIKNMDE SISCENILLTNYTHLILFLITKKYIIDGKSSLASKCIEVLEKMLPNSSDVTFYKFLNKQH SLYEQQFEFLKEVIQFRKNNEYDQYSQIGCNLLHYDLLISGLLFDVKSYDYSYQYFLKLD LANYFSELEIPDEYKMLINKYRENES
EMBL CDSEEI13070
Sequence length446 AA
Potential Application1) It can be a useful tool for glycoengineering as it can catalyze multiple linkages: Glc/Gal(-O)Ser/Thr, Glc/Gal(-S)Cys and Glc/Gal(beta)Glc/Gal(-O/S)Ser/Thr/Cys.
Additional Information1) EntS diglycosylates EC peptide (enterocin 96) in vitro with two hexoses at Ser33 residue.
2) EntS modifies ECS33C and ECS33T peptides at Cys33 and Thr33 residues, respectively, therefore displays O-glycosyltransferase activity as well as S-glycosyltransferase activity.
3) Site-directed mutagenesis (at multiple conserved sites including DXD motif) suggests that EntS utilises the single active site for both mono- and di-glycosyltransferase activities and DXD motif (DAD in this case) is a part of an active site.
4) EntS displays sequential dissociative mechanism for iterative di-glycosylation.
5) The stereochemistry of the terminal linkage catalysed by EntS has beta-configuration in di-glycosylated peptide and it does not require a secondary structure/N-terminal alpha-helix in peptide for glycosylation, as previously observed in case of SunS and ThuS.
Glycosyltransferase Information
Glycosylation TypeO- (Ser) linked and S- (Cys) linked 
CAZY FamilyGT2
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential dissociative
Acceptor specificity Sequon_1Minimal sequon: IHSLLNRLGG (D/E?G/R) (S/T/C≠Y/N) (S/T/R/A≠G/D)
Donor TypeNucleotide activated sugars
Donor SpecificityUDP-Glc is the most preferred substrate but it can accept UDP-Gal and GDP-Glc as well. Therefore, EntS has relaxed donor specificity.
Glycan Information
Glycan transferredMonosaccharides (Glc and Gal) 
Method of Glycan IndentificationLC-MS/MS
Experimental_strategiesIn vitro 
Acceptor Subtrate Information
Acceptor Substrate name Enterocin 96
ProGPdb ID ProGP552
Acceptor Substrate name ECS33C
Acceptor Substrate name ECS33T
Acceptor Substrate name ECD32E
Acceptor Substrate name EC∆D35
Acceptor Substrate name ECS34A
Acceptor Substrate name EC∆S34
Acceptor Substrate name ECS34R
Acceptor Substrate name ECS34T
Litrature
Year Of Validation2017 
Reference Nagar, R., & Rao, A. (2017). An iterative glycosyltransferase EntS catalyzes transfer and extension of O-and S-linked monosaccharide in enterocin 96. Glycobiology, 27(8), 766-776.

Authors Nagar, R., & Rao, A.
Research groupsCSIR-Institute of Microbial Technology, Sector 39A, Chandigarh-160036, India.
Corresponding Author Rao, A.
ContactsCSIR-Institute of Microbial Technology, Sector 39A, Chandigarh-160036, India.