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ProGlyProt ID
BC106
Organism Information
Organism Name
Bacillus subtilis 168
Domain
Bacteria
Classification
Family: Bacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
GenBank
EMBL
 
 
Gene Information
Gene Name
sunA
NCBI Gene ID
GenBank Gene Sequence
 
 
Protein Information
Protein Name
Sublansin
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
Sequence length
56 AA
Subcellular Location
Secreted
Function
SPβ prophage-derived bacteriocin sublancin-168. It has antimicrobial activity against Gram-positive bacteria. It is stable at both low and high pH and lacks free thiols.
 
 
Glycosylation Status
Glycosylation Type
S (Cys) linked
Experimentally Validated Glycosite(s) in Full Length Protein
(Propeptide: 1-19) C41
Experimentally Validated Glycosite(s ) in Mature Protein
C22
Glycosite(s) Annotated Protein Sequence
>sp|P68577|SUNA_BACSU SPBc2 prophage-derived bacteriocin sublancin-168 OS=Bacill
us subtilis GN=sunA PE=1 SV=1 MEKLFKEVKLEELENQKGSGLGKAQCAALWLQCASGGTIGC*(4
1)
GGGAVACQNYRQFCR
Sequence Around Glycosites (21 AA)
LQCASGGTIGCGGGAVACQNY
Technique(s) used for Glycosylation Detection
Higher mass observed using mass spectrometry
Technique(s) used for Glycosylated Residue(s) Detection
Tandem ESI-MS (electrospray ionization quadrupole-TOF mass spectrometry) analysis after chymotrypsin digestion.
Protein Glycosylation- Implication
Glucosylation is essential for its bioactivity.
 
 
Glycan Information
Glycan Annotation
UDP-Glc, UDP-GlcNAc, UDP-Gal, GDP-Man and UDP-Xyl can serve as substrates for SunS GTase but UDP-α-D-glucose is most efficiently used.
Technique(s) used for Glycan Identification
GC-MS (gas chromatography-mass spectrometry) analysis after trimethylsilylation
 
 
Protein Glycosylation linked (PGL) gene(s)
OST Gene Name
sunS or yolJ (BSU21450)
OST NCBI Gene ID
OST GenBank Gene Sequence
OST Protein Name
SPBc2 prophage-derived glycosyltransferase SunS
OST UniProtKB/ SwissProt ID
OST NCBI RefSeq
OST EMBL-CDS
OST UniProtKB Sequence
PGL Additional Links
 
 
Literature
Reference(s)
1) Oman, T.J., Boettcher, J.M., Wang, H., Okalibe, X.N. and van der Donk, W.A. (2011) Sublancin is not a lantibiotic but an S-linked glycopeptide. Nat Chem Biol, 7, 78-80. [PubMed: 21196935]
2) 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]
Additional Comments
SunS is a glycosyltransferase with very relaxed substrate specificity. It shows strong regioselectivity and chemoselectivity for glycosylation of a thiol.
S-linked glycosylation is very rare. It has been observed that cysteine glycosylation leads to the formation of more stable products (both at low and high pH) than does serine glycosylation.
Year of Identification
2011
Year of Validation
2011
 
 
Copyright @ 2011 IMTECH
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