Difference between revisions of "SunA"

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(Extended information on the protein)
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'''Additional publications:''' {{PubMed|20817675}}
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<pubmed>12884008,9722542 15743949,17720793,16306698, 19465659 21196935</pubmed>
 
<pubmed>12884008,9722542 15743949,17720793,16306698, 19465659 21196935</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:48, 16 September 2011

  • Description: sublancin 168 lantibiotic antimicrobial precursor peptide

Gene name sunA
Synonyms yolG
Essential no
Product sublancin 168 lantibiotic antimicrobial precursor peptide
Function antimicrobial peptide
MW, pI 5 kDa, 7.963
Gene length, protein length 168 bp, 56 aa
Immediate neighbours sunT, sunI
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SunA context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

miscellaneous metabolic pathways, biosynthesis of antibacterial compounds, 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:
  • Domains:
  • Modification: contains a glucose attached to a cysteine residue, glycosylation is essential for its antimicrobial activity PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • 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

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

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

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)

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)