Difference between revisions of "SunS"
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− | * '''Description:''' | + | * '''Description:''' sublancin S-glycosyltransferase <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
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− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || sublancin S-glycosyltransferase |
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− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of the antimicrobial peptide sublancin |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | ||
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* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
+ | ** selectively modifies Cys22 in a 56-amino acid peptide substrate [[SunA]] and can accept a variety of NDP-sugars {{PubMed|21196935}} | ||
* '''Protein family:''' EngA subfamily (according to Swiss-Prot) | * '''Protein family:''' EngA subfamily (according to Swiss-Prot) | ||
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Additional publications: {{PubMed|20817675}} | Additional publications: {{PubMed|20817675}} | ||
− | <pubmed>15743949 </pubmed> | + | <pubmed>15743949 21196935 21910430 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:46, 16 September 2011
- Description: sublancin S-glycosyltransferase
Gene name | yolJ |
Synonyms | |
Essential | no |
Product | sublancin S-glycosyltransferase |
Function | biosynthesis of the antimicrobial peptide sublancin |
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
MW, pI | 49 kDa, 5.33 |
Gene length, protein length | 1266 bp, 422 aa |
Immediate neighbours | bdbB, bdbA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
SP-beta prophage, membrane proteins, poorly characterized/ putative enzymes
This gene is a member of the following regulons
Abh regulon, AbrB regulon, Rok regulon, YvrHb regulon
The gene
Basic information
- Locus tag: BSU21450
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: EngA subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O31986
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
Huan Wang, Wilfred A van der Donk
Substrate selectivity of the sublancin S-glycosyltransferase.
J Am Chem Soc: 2011, 133(41);16394-7
[PubMed:21910430]
[WorldCat.org]
[DOI]
(I p)
Trent J Oman, John M Boettcher, Huan Wang, Xenia N Okalibe, Wilfred A van der Donk
Sublancin is not a lantibiotic but an S-linked glycopeptide.
Nat Chem Biol: 2011, 7(2);78-80
[PubMed:21196935]
[WorldCat.org]
[DOI]
(I p)
Mark Albano, Wiep Klaas Smits, Linh T Y Ho, Barbara Kraigher, Ines Mandic-Mulec, Oscar P Kuipers, David Dubnau
The Rok protein of Bacillus subtilis represses genes for cell surface and extracellular functions.
J Bacteriol: 2005, 187(6);2010-9
[PubMed:15743949]
[WorldCat.org]
[DOI]
(P p)