ProGP404

Home -> ProGPdb -> Search ProGP -> Display data

ProGP ID ProGP404
Validation Status Characterized
Organism Information
Organism NameBacillus subtilis 168
Domain Bacteria
Classification Family: Bacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 1423
Genome Sequence(s)
GenBank AF014938.1
EMBL AF014938
Gene Information
Gene NamesunA
NCBI Gene ID 939121
GenBank Gene Sequence 939121
Protein Information
Protein NameSublansin
UniProtKB/SwissProt ID P68577
NCBI RefSeq NP_390031.1
EMBL-CDSAAC63531.1
UniProtKB Sequence >sp|P68577|SUNA_BACSU SPBc2 prophage-derived bacteriocin sublancin-168 OS=Bacillus subtilis GN=sunA PE=1 SV=1 MEKLFKEVKLEELENQKGSGLGKAQCAALWLQCASGGTIGCGGGAVACQNYRQFCR
Sequence length 56 AA
Subcellular LocationSecreted
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 ProteinC22
Glycosite(s) Annotated Protein Sequence >sp|P68577|SUNA_BACSU SPBc2 prophage-derived bacteriocin sublancin-168 OS=Bacillus subtilis GN=sunA PE=1 SV=1 MEKLFKEVKLEELENQKGSGLGKAQCAALWLQCASGGTIGC*(41)GGGAVACQNYRQFCR
Sequence Around Glycosites (21 AA) LQCASGGTIGCGGGAVACQNY
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionHigher 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 ProGT IDProGT47
Characterized Accessory Gene(s)SunS is a glycosyltransferase with very relaxed substrate specificity. It shows strong regioselectivity and chemoselectivity for glycosylation of a thiol.
Literature
Additional CommentS-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 Identification2011
Year of Identification Month Wise2011.02
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. 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 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 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.
Reference1) 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]
AuthorOman, T.J., Boettcher, J.M., Wang, H., Okalibe, X.N. and van der Donk, W.A.
Research GroupDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA
Corresponding Author van der Donk, W.A.
ContactDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA