Difference between revisions of "YrhJ"

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(Categories containing this gene/protein)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:'''
+
* '''[[SubtInteract|Interactions]]:'''
  
* '''Localization:''' cell membrane (according to Swiss-Prot)
+
* '''[[Localization]]:'''
 +
** cell membrane (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Regulation:'''  
 
* '''Regulation:'''  
 
** induced by unsaturated fatty acids ([[FatR]]) {{PubMed|11734890}}  
 
** induced by unsaturated fatty acids ([[FatR]]) {{PubMed|11734890}}  
 +
** expression is reduced in a [[SigV]] mutant {{PubMed|21926231}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
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=References=
 
=References=
 
+
'''Additional publications:''' {{PubMed|21926231}}
 
<pubmed>11734890,10917605 ,11574077,14741768,15122913, 12775685 16716428 16381045 20525796 12207695 9636707</pubmed>
 
<pubmed>11734890,10917605 ,11574077,14741768,15122913, 12775685 16716428 16381045 20525796 12207695 9636707</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:19, 16 October 2011

Gene name yrhJ
Synonyms cypE
Essential no
Product NADPH-cytochrome P450 reductase
Function fatty acid metabolism
MW, pI 118 kDa, 6.017
Gene length, protein length 3162 bp, 1054 aa
Immediate neighbours yrhK, fatR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YrhJ context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

electron transport/ other, lipid metabolism/ other, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins

This gene is a member of the following regulons

FatR regulon, SigM regulon, SigW regulon, SigX regulon

The gene

Basic information

  • Locus tag: BSU27160

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • hydroxylates medium-chain fatty acids in subterminal positions PubMed
  • Protein family:
  • Paralogous protein(s): YetO

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2X7Y (from Bacillus megaterium; 67% identity, 88% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:

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

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Sabine Eiben, Leonard Kaysser, Steffen Maurer, Katja Kühnel, Vlada B Urlacher, Rolf D Schmid
Preparative use of isolated CYP102 monooxygenases -- a critical appraisal.
J Biotechnol: 2006, 124(4);662-9
[PubMed:16716428] [WorldCat.org] [DOI] (P p)

Oliver Lentz, Anton Feenstra, Tilo Habicher, Bernhard Hauer, Rolf D Schmid, Vlada B Urlacher
Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system.
Chembiochem: 2006, 7(2);345-50
[PubMed:16381045] [WorldCat.org] [DOI] (P p)

Mattias C U Gustafsson, Olivier Roitel, Ker R Marshall, Michael A Noble, Stephen K Chapman, Antonio Pessegueiro, Armand J Fulco, Myles R Cheesman, Claes von Wachenfeldt, Andrew W Munro
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
Biochemistry: 2004, 43(18);5474-87
[PubMed:15122913] [WorldCat.org] [DOI] (P p)

Oliver Lentz, Vlada Urlacher, Rolf D Schmid
Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis.
J Biotechnol: 2004, 108(1);41-9
[PubMed:14741768] [WorldCat.org] [DOI] (P p)

Penny D Thackray, Anne Moir
SigM, an extracytoplasmic function sigma factor of Bacillus subtilis, is activated in response to cell wall antibiotics, ethanol, heat, acid, and superoxide stress.
J Bacteriol: 2003, 185(12);3491-8
[PubMed:12775685] [WorldCat.org] [DOI] (P p)

Min Cao, Tao Wang, Rick Ye, John D Helmann
Antibiotics that inhibit cell wall biosynthesis induce expression of the Bacillus subtilis sigma(W) and sigma(M) regulons.
Mol Microbiol: 2002, 45(5);1267-76
[PubMed:12207695] [WorldCat.org] [DOI] (P p)

M C Gustafsson, C N Palmer, C R Wolf, C von Wachenfeldt
Fatty-acid-displaced transcriptional repressor, a conserved regulator of cytochrome P450 102 transcription in Bacillus species.
Arch Microbiol: 2001, 176(6);459-64
[PubMed:11734890] [WorldCat.org] [DOI] (P p)

T R Lee, H P Hsu, G C Shaw
Transcriptional regulation of the Bacillus subtilis bscR-CYP102A3 operon by the BscR repressor and differential induction of cytochrome CYP102A3 expression by oleic acid and palmitate.
J Biochem: 2001, 130(4);569-74
[PubMed:11574077] [WorldCat.org] [DOI] (P p)

C N Palmer, M C Gustafsson, H Dobson, C von Wachenfeldt, C R Wolf
Adaptive responses to fatty acids are mediated by the regulated expression of cytochromes P450.
Biochem Soc Trans: 1999, 27(4);374-8
[PubMed:10917605] [WorldCat.org] [DOI] (P p)

X Huang, J D Helmann
Identification of target promoters for the Bacillus subtilis sigma X factor using a consensus-directed search.
J Mol Biol: 1998, 279(1);165-73
[PubMed:9636707] [WorldCat.org] [DOI] (P p)