Difference between revisions of "SigX"

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* '''Description:''' RNA polymerase ECF-type [[sigma factor]] SigX <br/><br/>
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* '''Description:''' [[RNA polymerase]] ECF-type [[sigma factor]] SigX <br/><br/>
  
 
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{| 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''' || RNA polymerase ECF-type [[sigma factor]] SigX
+
|style="background:#ABCDEF;" align="center"| '''Product''' || [[RNA polymerase]] ECF-type [[sigma factor]] SigX
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || cell surface properties
 
|style="background:#ABCDEF;" align="center"|'''Function''' || cell surface properties

Revision as of 18:08, 21 August 2010

Gene name sigX
Synonyms ypuM
Essential no
Product RNA polymerase ECF-type sigma factor SigX
Function cell surface properties
MW, pI 23 kDa, 6.086
Gene length, protein length 582 bp, 194 aa
Immediate neighbours rsiX, resE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SigX context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU23100

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: ECF subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Genes controlled by SigX

abh, pbpX, csbB, abh, dltA-dltB-dltC-dltD-dltE

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:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • 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

Ewan J Murray, Mark A Strauch, Nicola R Stanley-Wall
SigmaX is involved in controlling Bacillus subtilis biofilm architecture through the AbrB homologue Abh.
J Bacteriol: 2009, 191(22);6822-32
[PubMed:19767430] [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)

Warawan Eiamphungporn, John D Helmann
Extracytoplasmic function sigma factors regulate expression of the Bacillus subtilis yabE gene via a cis-acting antisense RNA.
J Bacteriol: 2009, 191(3);1101-5
[PubMed:19047346] [WorldCat.org] [DOI] (I p)

Thorsten Mascher, Anna-Barbara Hachmann, John D Helmann
Regulatory overlap and functional redundancy among Bacillus subtilis extracytoplasmic function sigma factors.
J Bacteriol: 2007, 189(19);6919-27
[PubMed:17675383] [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)

Mika Yoshimura, Kei Asai, Yoshito Sadaie, Hirofumi Yoshikawa
Interaction of Bacillus subtilis extracytoplasmic function (ECF) sigma factors with the N-terminal regions of their potential anti-sigma factors.
Microbiology (Reading): 2004, 150(Pt 3);591-599
[PubMed:14993308] [WorldCat.org] [DOI] (P p)

Min Cao, John D Helmann
The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.
J Bacteriol: 2004, 186(4);1136-46
[PubMed:14762009] [WorldCat.org] [DOI] (P p)

Thorsten Mascher, Neil G Margulis, Tao Wang, Rick W Ye, John D Helmann
Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon.
Mol Microbiol: 2003, 50(5);1591-604
[PubMed:14651641] [WorldCat.org] [DOI] (P p)

Min Cao, John D Helmann
Regulation of the Bacillus subtilis bcrC bacitracin resistance gene by two extracytoplasmic function sigma factors.
J Bacteriol: 2002, 184(22);6123-9
[PubMed:12399481] [WorldCat.org] [DOI] (P p)

J Qiu, J D Helmann
The -10 region is a key promoter specificity determinant for the Bacillus subtilis extracytoplasmic-function sigma factors sigma(X) and sigma(W).
J Bacteriol: 2001, 183(6);1921-7
[PubMed:11222589] [WorldCat.org] [DOI] (P p)

M S Turner, J D Helmann
Mutations in multidrug efflux homologs, sugar isomerases, and antimicrobial biosynthesis genes differentially elevate activity of the sigma(X) and sigma(W) factors in Bacillus subtilis.
J Bacteriol: 2000, 182(18);5202-10
[PubMed:10960106] [WorldCat.org] [DOI] (P p)

X Huang, K L Fredrick, J D Helmann
Promoter recognition by Bacillus subtilis sigmaW: autoregulation and partial overlap with the sigmaX regulon.
J Bacteriol: 1998, 180(15);3765-70
[PubMed:9683469] [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)

S Brutsche, V Braun
SigX of Bacillus subtilis replaces the ECF sigma factor fecI of Escherichia coli and is inhibited by RsiX.
Mol Gen Genet: 1997, 256(4);416-25
[PubMed:9393439] [WorldCat.org] [DOI] (P p)

X Huang, A Decatur, A Sorokin, J D Helmann
The Bacillus subtilis sigma(X) protein is an extracytoplasmic function sigma factor contributing to survival at high temperature.
J Bacteriol: 1997, 179(9);2915-21
[PubMed:9139908] [WorldCat.org] [DOI] (P p)

V Azevedo, A Sorokin, S D Ehrlich, P Serror
The transcriptional organization of the Bacillus subtilis 168 chromosome region between the spoVAF and serA genetic loci.
Mol Microbiol: 1993, 10(2);397-405
[PubMed:7934830] [WorldCat.org] [DOI] (P p)