Difference between revisions of "SunA"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
Line 65: Line 65:
  
 
=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
Line 129: Line 126:
 
=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' GP1563 (aphA3), available in [[Stülke]] lab
+
* '''Mutant:'''  
 +
** GP1563 (aphA3), available in [[ Jörg Stülke]]'s lab
 +
** GP1565 (''[[sunA]]-[[sunI]]'', aphA3), available in [[ Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 10:31, 31 January 2014

  • Description: sublancin 168 lantibiotic antimicrobial precursor peptide

Gene name sunA
Synonyms yolG
Essential no
Product sublancin 168 lantibiotic antimicrobial precursor peptide
Function antimicrobial peptide
Gene expression levels in SubtiExpress: sunA
MW, pI 5 kDa, 7.963
Gene length, protein length 168 bp, 56 aa
Immediate neighbours sunT, sunI
Sequences Protein DNA DNA_with_flanks
Genetic context
SunA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SunA expression.png















Categories containing this gene/protein

miscellaneous metabolic pathways, biosynthesis of antibacterial compounds, toxins, antitoxins and immunity against toxins, SP-beta prophage, membrane proteins

This gene is a member of the following regulons

Abh regulon, AbrB regulon, Rok regulon, YvrHb regulon

The gene

Basic information

  • Locus tag: BSU21480

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: IPP isomerase type 2 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification: contains a glucose attached to a cysteine residue, glycosylation is essential for its antimicrobial activity PubMed
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information: the mRNA is very stable (half-life > 15 min) PubMed

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Chantal V Garcia De Gonzalo, Lingyang Zhu, Trent J Oman, Wilfred A van der Donk
NMR structure of the S-linked glycopeptide sublancin 168.
ACS Chem Biol: 2014, 9(3);796-801
[PubMed:24405370] [WorldCat.org] [DOI] (I p)

Rebecca Mendez, Alba Gutierrez, Jasmin Reyes, Leticia Márquez-Magaña
The extracytoplasmic function sigma factor SigY is important for efficient maintenance of the Spβ prophage that encodes sublancin in Bacillus subtilis.
DNA Cell Biol: 2012, 31(6);946-55
[PubMed:22400495] [WorldCat.org] [DOI] (I p)

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)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Yun Luo, John D Helmann
Extracytoplasmic function sigma factors with overlapping promoter specificity regulate sublancin production in Bacillus subtilis.
J Bacteriol: 2009, 191(15);4951-8
[PubMed:19465659] [WorldCat.org] [DOI] (I p)

Mark A Strauch, Benjamin G Bobay, John Cavanagh, Fude Yao, Angelo Wilson, Yoann Le Breton
Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.
J Bacteriol: 2007, 189(21);7720-32
[PubMed:17720793] [WorldCat.org] [DOI] (P p)

Masakuni Serizawa, Keisuke Kodama, Hiroki Yamamoto, Kazuo Kobayashi, Naotake Ogasawara, Junichi Sekiguchi
Functional analysis of the YvrGHb two-component system of Bacillus subtilis: identification of the regulated genes by DNA microarray and northern blot analyses.
Biosci Biotechnol Biochem: 2005, 69(11);2155-69
[PubMed:16306698] [WorldCat.org] [DOI] (P 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)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

S H Paik, A Chakicherla, J N Hansen
Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168.
J Biol Chem: 1998, 273(36);23134-42
[PubMed:9722542] [WorldCat.org] [DOI] (P p)