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ProGlyProt ID
BC150
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)
 
 
Genome Sequence(s)
EMBL
 
 
Gene Information
Gene Name
gccF
 
 
Protein Information
Protein Name
Glycocin F
UniProtKB/SwissProt ID
EMBL-CDS
UniProtKB Sequence
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
 
 
Glycosylation Status
Glycosylation Type
O (Ser) linked 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)GTCDYMYSHCFGIK
HHSSGSS 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: β-GlcNAc-Ser, β-GlcNAc-Cys.
Two N-Acetylglucosamines present. One is β-O-linked to Ser18 while the other one is S-linked to C-terminal Cys43.
Technique(s) used for Glycan Identification
N-acetyl-β-D-glucosaminidase GcnA treatment and NMR (nuclear magnetic resonance) spectroscopy
 
 
Protein Glycosylation linked (PGL) gene(s)
Predicted Accessory Gene(s)
Glycosyltransferase GccA (encoded in the gcc gene cluster) glycosylates Ser18 and/or Cys43 of preglycocin F.
 
 
Literature
Reference(s)
1) 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]
2) 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]
Additional Comments
N-GlcNAc-Cys is a novel type of linkage.
Year of Identification
2011
Year of Validation
2011
 
 
Copyright @ 2011 IMTECH
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