ProGP402 (Glycocin F)
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ProGP ID | ProGP402 (Glycocin F) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Lactobacillus plantarum KW30 |
Domain | Bacteria |
Classification | Family: Lactobacillaceae Order: Lactobacillales Class: Bacilli (or Firmibacteria) Division or phylum: "Firmicutes" |
Taxonomic ID (NCBI) | 1590 |
Genome Information | |
GenBank | GU552553 |
EMBL | GU552553 |
Gene Information | |
Gene Name | gccF |
Protein Information | |
Protein Name | Glycocin F |
UniProtKB/SwissProt ID | E9K9Z1 |
EMBL-CDS | ADV57366.1 |
UniProtKB Sequence | >tr|E9K9Z1|E9K9Z1_LACPL Prebacteriocin glycocin F OS=Lactobacillus plantarum GN=gccF PE=4 SV=1 MSKLVKTLTISEISKAQNNGGKPAWCWYTLAMCGAGYDSGTCDYMYSHCFGIKHHSSGSS SYHC |
Sequence length | 64 AA |
Subcellular Location | Secreted |
Function | Glycocin F is a bacteriocin that possesses bacteriostatic activity. This activity is reversed by free N-acetylglucosamine. |
Protein Structure | |
PDB ID | 2KUY |
Glycosylation Status | |
Glycosylation Type | O- (Ser) and S- (Cys) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | (Signal peptide: 1-21) S39, C64 |
Experimentally Validated Glycosite(s ) in Mature Protein | S18, C43 |
Glycosite(s) Annotated Protein Sequence | >tr|E9K9Z1|E9K9Z1_LACPL Prebacteriocin glycocin F OS=Lactobacillus plantarum GN=gccF PE=4 SV=1 MSKLVKTLTISEISKAQNNGGKPAWCWYTLAMCGAGYDS*(39)GTCDYMYSHCFGIKHHSSGSS SYHC*(64) |
Sequence Around Glycosites (21 AA) | TLAMCGAGYDSGTCDYMYSHC
HHSSGSSSYHC |
Technique(s) used for Glycosylation Detection | Mass difference measured and accounted for by Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) with electron capture dissociation (ECD) |
Technique(s) used for Glycosylated Residue(s) Detection | Edman sequencing and Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) |
Protein Glycosylation- Implication | O-linked N-acetylglucosamine is required for bacteriostatic activity. |
Glycan Information | |
Glycan Annotation | Linkages: ?-GlcNAc-Ser, HexNAc-Cys. N-Acetylglucosamine is ?-O-linked to Ser18 and N-acetylhexosamine is S-linked to C-terminal Cys43. |
Technique(s) used for Glycan Identification | N-acetyl-?-D-glucosaminidase GcnA treatment. |
Literature | |
Year of Identification | 2011 |
Year of Identification Month Wise | 2011.5.20 |
Year of Validation | 2011 |
Reference | Stepper, J., Shastri, S., Loo, T.S., Preston, J.C., Novak, P., Man, P., Moore, C.H., Havlicek, V., Patchett, M.L. and Norris, G.E. (2011) Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins. FEBS Lett, 585, 645-650. [PubMed: 21251913] |
Author | Stepper, J., Shastri, S., Loo, T.S., Preston, J.C., Novak, P., Man, P., Moore, C.H., Havlicek, V., Patchett, M.L. and Norris, G.E. |
Research Group | Institute of Molecular Biosciences, Massey University, Palmerston North, New Zealand. |
Corresponding Author | Norris, G.E |
Contact | Institute of Molecular Biosciences, Massey University, Palmerston North, New Zealand. |
Reference | Venugopal, H., Edwards, P.J., Schwalbe, M., Claridge, J.K., Libich, D.S., Stepper, J., Loo, T., Patchett, M.L., Norris, G.E. and Pascal, S.M. (2011) Structural, dynamic, and chemical characterization of a novel S-glycosylated bacteriocin. Biochemistry, 50, 2748-2755. [PubMed: 21395300] |
Author | Venugopal, H., Edwards, P.J., Schwalbe, M., Claridge, J.K., Libich, D.S., Stepper, J., Loo, T., Patchett, M.L., Norris, G.E. Pascal, S.M. |
Research Group | Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand |
Corresponding Author | Pascal, S.M. |
Contact | Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand |