TrxA

• Description: antioxidative action by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange
  
  

Gene name	trxA
Synonyms	trx
Essential	yes PubMed
Product	thioredoxin
Function	protection of proteins against oxidative damage
MW, pI	11 kDa, 4.308
Gene length, protein length	312 bp, 104 aa
Immediate neighbours	uvrC, abf2
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU28500

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: thioredoxin family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: ArsC-TrxA PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 2GZZ (oxidized form), 2GZY (reduced form), 2IPA (TrxA-ArsC-complex) PubMed

• UniProt: P14949

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: trxA PubMed

• Sigma factor: SigA PubMed, SigB PubMed

• Regulation:
  • induced by stress (SigB) PubMed
  • regulation by Spx in response to diamide stress
  • induced by heat stress (CtsR) PubMed

• Regulatory mechanism:
  • CtsR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Michiko M Nakano, Ann Lin, Cole S Zuber, Kate J Newberry, Richard G Brennan, Peter Zuber
Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase alpha subunit.
PLoS One: 2010, 5(1);e8664
[PubMed:20084284] [WorldCat.org] [DOI] (I e)

Dindo Y Reyes, Peter Zuber
Activation of transcription initiation by Spx: formation of transcription complex and identification of a Cis-acting element required for transcriptional activation.
Mol Microbiol: 2008, 69(3);765-79
[PubMed:18687074] [WorldCat.org] [DOI] (I p)

Jörg Mostertz, Falko Hochgräfe, Britta Jürgen, Thomas Schweder, Michael Hecker
The role of thioredoxin TrxA in Bacillus subtilis: a proteomics and transcriptomics approach.
Proteomics: 2008, 8(13);2676-90
[PubMed:18601268] [WorldCat.org] [DOI] (I p)

Mirja Carlsson Möller, Lars Hederstedt
Extracytoplasmic processes impaired by inactivation of trxA (thioredoxin gene) in Bacillus subtilis.
J Bacteriol: 2008, 190(13);4660-5
[PubMed:18456801] [WorldCat.org] [DOI] (I p)

You Li, Yunfei Hu, Xinxin Zhang, Huimin Xu, Ewen Lescop, Bin Xia, Changwen Jin
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis.
J Biol Chem: 2007, 282(15);11078-83
[PubMed:17303556] [WorldCat.org] [DOI] (P p)

Wiep Klaas Smits, Jean-Yves F Dubois, Sierd Bron, Jan Maarten van Dijl, Oscar P Kuipers
Tricksy business: transcriptome analysis reveals the involvement of thioredoxin A in redox homeostasis, oxidative stress, sulfur metabolism, and cellular differentiation in Bacillus subtilis.
J Bacteriol: 2005, 187(12);3921-30
[PubMed:15937154] [WorldCat.org] [DOI] (P p)

Shunji Nakano, Michiko M Nakano, Ying Zhang, Montira Leelakriangsak, Peter Zuber
A regulatory protein that interferes with activator-stimulated transcription in bacteria.
Proc Natl Acad Sci U S A: 2003, 100(7);4233-8
[PubMed:12642660] [WorldCat.org] [DOI] (P p)

A Petersohn, M Brigulla, S Haas, J D Hoheisel, U Völker, M Hecker
Global analysis of the general stress response of Bacillus subtilis.
J Bacteriol: 2001, 183(19);5617-31
[PubMed:11544224] [WorldCat.org] [DOI] (P p)

E Krüger, M Hecker
The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes.
J Bacteriol: 1998, 180(24);6681-8
[PubMed:9852015] [WorldCat.org] [DOI] (P p)

C Scharf, S Riethdorf, H Ernst, S Engelmann, U Völker, M Hecker
Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis.
J Bacteriol: 1998, 180(7);1869-77
[PubMed:9537387] [WorldCat.org] [DOI] (P p)