TrxA

• Description: thioredoxin, 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
Gene expression levels in SubtiExpress: trxA
Interactions involving this protein in SubtInteract: TrxA
MW, pI	11 kDa, 4.308
Gene length, protein length	312 bp, 104 aa
Immediate neighbours	uvrC, abf2
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

electron transport/ other, general stress proteins (controlled by SigB), resistance against oxidative and electrophile stress, essential genes

This gene is a member of the following regulons

CtsR regulon, SigB regulon, Spx regulon

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:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • ArsC-TrxA PubMed

• Localization: cytoplasm PubMed

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

• Expression browser: 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:
  • A ncRNA is predicted between trxA and abf2 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Mackenzie J Parker, Xuling Zhu, JoAnne Stubbe
Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.
Biochemistry: 2014, 53(4);766-76
[PubMed:24401092] [WorldCat.org] [DOI] (I p)

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)

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)

Thijs R H M Kouwen, Annemieke van der Goot, Ronald Dorenbos, Theresa Winter, Haike Antelmann, Marie-Claire Plaisier, Wim J Quax, January Maarten van Dijl, Jean-Yves F Dubois
Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria.
Mol Microbiol: 2007, 64(4);984-99
[PubMed:17501922] [WorldCat.org] [DOI] (P 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)