ProGP552 (Hypothetical protein but identical to entrocin96 of Enterococcus faecalis WHE96)

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ProGP ID ProGP552 (Hypothetical protein but identical to entrocin96 of Enterococcus faecalis WHE96)
Validation Status Characterized
Organism Information
Organism NameEnterococcus faecalis TX0104
Domain Bacteria
Classification Family:Enterococcaceae
Order: Lactobacillales
Class: Bacilli
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 491074
Genome Information
GenBank GG668924.1
EMBL GG668924.1
Gene Information
Gene NameHMPREF0348_0422
GenBank Gene Sequence ACGL01000031.1
Protein Information
Protein NameHypothetical protein but identical to entrocin96 of Enterococcus faecalis WHE96
UniProtKB/SwissProt ID C0X1N7
NCBI RefSeq WP_002382828
UniProtKB Sequence >tr|C0X1N7|C0X1N7_ENTFL Uncharacterized protein OS=Enterococcus faecalis TX0104 GN=HMPREF0348_0422 PE=4 SV=1 MERTKGDNTMLNKKLLENGVVNAVTIDELDAQFGGMSKRDCNLMKACCAGQAVTYAIHSLLNRLGGDSSDPAGCNDIVRKYCK
Sequence length 83 AA
Glycosylation Status
Glycosylation Type O- (Ser) and S- (Cys) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS33 (C33 when S33 replaced with C33)
Glycosite(s) Annotated Protein Sequence >tr|C0X1N7|C0X1N7_ENTFL Uncharacterized protein OS=Enterococcus faecalis TX0104 GN=HMPREF0348_0422 PE=4 SV=1 MERTKGDNTMLNKKLLENGVVNAVTIDELDAQFGGMSKRDCNLMKACCAGQAVTYAIHSLLNRLGGDS*(33)SDPAGCNDIVRKYCK
Sequence Around Glycosites (21 AA) HSLLNRLGGDSSDPAGCNDIV
Technique(s) used for Glycosylated Residue(s) Detection LC ESI-MS, MALDI-TOF MS and tandem MS
Protein Glycosylation- Implication It is a di-glycosylated bacteriocin and active in glucosylated form only.Its antimicrobial activity affected by both nature and number of sugars attached to EC peptide affect its bioactivity against Listeria species
Glycan Information
Glycan Annotation single- and double glucosylated ( glucose and galactose
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameEntS
OST ProGT IDProGT116 (EntS)
Literature
ReferenceNagar, R. and Rao, A., 2017. An iterative glycosyltransferase EntS catalyzes transfer and extension of O-and S-linked monosaccharide in enterocin 96. Glycobiology, 27(8), pp.766-776.
Corresponding Author Alka Rao
ContactCSIR-Institute of Microbial Technology, Sector 39A, Chandigarh 160036, India
ReferenceNagar R, Rao A (2017) An iterative glycosyltransferase EntS catalyzes transfer and extension of O- and S-linked monosaccharide in enterocin 96. Glycobiology, 12. [PubMed: 28498962]
AuthorNagar R, Rao A
Research GroupCSIR-Institute of Microbial Technology, Sector 39A, Chandigarh-160036, India.
Corresponding Author Rao A
ContactCSIR-Institute of Microbial Technology, Sector 39A, Chandigarh-160036, India.