ProGP406

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ProGP ID ProGP406
Validation Status Characterized
Organism Information
Organism NameLactobacillus plantarum KW30
Domain Bacteria
Classification Family: Lactobacillaceae
Order: Lactobacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 1590
Genome Sequence(s)
GenBank GU552553
EMBL GU552553
Gene Information
Gene NamegccF
Protein Information
Protein NameGlycocin F
UniProtKB/SwissProt ID E9K9Z1
EMBL-CDSADV57366.1
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 LocationSecreted
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 ProteinS18, 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 DetectionMass 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: β-GlcNAc-Ser, HexNAc-Cys.
N-Acetylglucosamine is β-O-linked to Ser18 and N-acetylhexosamine is S-linked to C-terminal Cys43.
Technique(s) used for Glycan Identification N-acetyl-β-D-glucosaminidase GcnA treatment.
Literature
Year of Identification2011
Year of Identification Month Wise2011.5.20
Year of Validation 2011
ReferenceStepper, 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. (201Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins. FEBS Lett, 585, 645-650. [PubMed: 21251913]
AuthorStepper, 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 GroupInstitute of Molecular Biosciences, Massey University, Palmerston North, New Zealand.
Corresponding Author Norris, G.E
ContactInstitute 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 GroupInstitute of Fundamental Sciences, Massey University, Palmerston North, New Zealand
Corresponding Author Pascal, S.M.
ContactInstitute of Fundamental Sciences, Massey University, Palmerston North, New Zealand