SigM

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Gene name sigM
Synonyms yhdM
Essential no
Product RNA polymerase ECF-type sigma factor SigM
Function responsible for intrinsic resistance against beta-lactam antibiotics
Gene expression levels in SubtiExpress: sigM
Interactions involving this protein in SubtInteract: SigM
MW, pI 19 kDa, 6.77
Gene length, protein length 489 bp, 163 aa
Immediate neighbours yhdL, yhdN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SigM context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SigM expression.png
















Categories containing this gene/protein

transcription, sigma factors and their control, cell envelope stress proteins (controlled by SigM, V, W, X, Y), resistance against toxins/ antibiotics

This gene is a member of the following regulons

SigM regulon

The SigM regulon

The gene

Basic information

  • Locus tag: BSU09520

Phenotypes of a mutant

  • SigM is essential for growth and survival in nutrient broth (NB) containing 1.4 M NaCl PubMed
  • sigM mutants form aberrantly shaped cells, which swell and lyse spontaneously during growth in NB medium containing increased levels (0.35-0.7 M) of a wide range of different salts PubMed
  • increased sensitivity towards beta-lactam antibiotics PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: sigma-70 factor family, ECF subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • 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

John Helmann, Cornell University, USA Homepage

Your additional remarks

References

Additional publications: PubMed

The SigM regulon

Other original publications

Satoshi Matsuoka, Minako Chiba, Yu Tanimura, Michihiro Hashimoto, Hiroshi Hara, Kouji Matsumoto
Abnormal morphology of Bacillus subtilis ugtP mutant cells lacking glucolipids.
Genes Genet Syst: 2011, 86(5);295-304
[PubMed:22362028] [WorldCat.org] [DOI] (I p)

Andriansjah Rukmana, Takuya Morimoto, Hiroki Takahashi, Giyanto, Naotake Ogasawara
Assessment of transcriptional responses of Bacillus subtilis cells to the antibiotic enduracidin, which interferes with cell wall synthesis, using a high-density tiling chip.
Genes Genet Syst: 2009, 84(4);253-67
[PubMed:20057163] [WorldCat.org] [DOI] (P p)

Michihiro Hashimoto, Hiroaki Takahashi, Yoshinori Hara, Hiroshi Hara, Kei Asai, Yoshito Sadaie, Kouji Matsumoto
Induction of extracytoplasmic function sigma factors in Bacillus subtilis cells with membranes of reduced phosphatidylglycerol content.
Genes Genet Syst: 2009, 84(3);191-8
[PubMed:19745567] [WorldCat.org] [DOI] (P 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)

Letal I Salzberg, John D Helmann
Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition.
J Bacteriol: 2008, 190(23);7797-807
[PubMed:18820022] [WorldCat.org] [DOI] (I p)

Eva Rietkötter, Diana Hoyer, Thorsten Mascher
Bacitracin sensing in Bacillus subtilis.
Mol Microbiol: 2008, 68(3);768-85
[PubMed:18394148] [WorldCat.org] [DOI] (I p)

Kathrin Minnig, Vladimir Lazarevic, Blazenka Soldo, Catherine Mauël
Analysis of teichoic acid biosynthesis regulation reveals that the extracytoplasmic function sigma factor sigmaM is induced by phosphate depletion in Bacillus subtilis W23.
Microbiology (Reading): 2005, 151(Pt 9);3041-3049
[PubMed:16151214] [WorldCat.org] [DOI] (P p)

Min Cao, Charles M Moore, John D Helmann
Bacillus subtilis paraquat resistance is directed by sigmaM, an extracytoplasmic function sigma factor, and is conferred by YqjL and BcrC.
J Bacteriol: 2005, 187(9);2948-56
[PubMed:15838020] [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)

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)

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, 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)

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 J Horsburgh, A Moir
Sigma M, an ECF RNA polymerase sigma factor of Bacillus subtilis 168, is essential for growth and survival in high concentrations of salt.
Mol Microbiol: 1999, 32(1);41-50
[PubMed:10216858] [WorldCat.org] [DOI] (P p)