P39914 · BRXC_BACSU

Function

function

S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a monothiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) GapA and GapB in vivo and probably a number of other oxidized cytosolic proteins. Debacillithiolates the S-bacillithiolated Bdr (Bdr-SSB) and BrxB (BrxB-SSB) in vitro. Involved in maintaining redox homeostasis in response to disulfide stress conditions.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionenzyme binding
Molecular Functionoxidoreductase activity
Molecular Functiontranslation elongation factor binding
Biological Processcell redox homeostasis
Biological Processresponse to oxidative stress

Keywords

Enzyme and pathway databases

Community curation (1)

Community annotation

Monothiol bacilliredoxin.

SourceSubmission dateContributor
PubMed:337225700000-0001-6837-2941

Names & Taxonomy

Protein names

  • Recommended name
    Monothiol bacilliredoxin BrxC
  • Short names
    Monothiol Brx-C
  • Alternative names
    • Bacillithiol system redox-active protein YtxJ
    • ORF2
    • ORF3

Gene names

    • Name
      brxC
    • Synonyms
      ytxJ
    • ORF names
      HIR78_17325
    • Ordered locus names
      BSU29760
Community curation (1)

Community suggested name: YtxJ

SourceSubmission dateContributor
PubMed:337225700000-0001-6837-2941

Organism names

  • Taxonomic identifier
  • Strains
    • 168
    • 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / NRRL NRS-744 / VKM B-501
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    P39914
  • Secondary accessions
    • A0A6M4JNQ9

Proteomes

Phenotypes & Variants

Disruption phenotype

Cells lacking the operon including this gene (ytxGH-brxC) have increased S-bacillithiolation of glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) GapA and GapB in cells with increased basal levels of oxidative stress due to concomitant deletion of genes encoding for catalase (katA) and alkyl hydroperoxide reductase (ahpCF).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis31Loss of debacillithiolation of S-bacillithiolated Bdr (Bdr-SSB).

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000499061-108Monothiol bacilliredoxin BrxC
Modified residue31S-bacillithiol cysteine disulfide

Post-translational modification

Cys can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation protects Cys residues against overoxidation by acting as a redox switch in response to oxidative stress.

Proteomic databases

Interaction

Subunit

Interacts with AbrB, BdhA, Bdr, BrxB, FolD, GapA, GapB, GatA, PfkA, PyrAA, PyrAB, PyrE, PyrG, PyrH, RpsB, RpsK, RpsL, SalA, SucC, Tuf and YtsJ.

Protein-protein interaction databases

Structure

Family & Domains

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    108
  • Mass (Da)
    12,402
  • Last updated
    1995-02-01 v1
  • Checksum
    D8F03DD68E79AF38
MAKQLIQSEEEFKRIAEQEGVFVFLKHSTTCPISQAAFHEFDAFANQHEDVPAYYLQVQEARPLSNFIAETYGVKHESPQIFIIQNGEVKWHTSHSQITEAAIEQHLS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X65945
EMBL· GenBank· DDBJ
CAA46762.1
EMBL· GenBank· DDBJ
Genomic DNA
AF008220
EMBL· GenBank· DDBJ
AAC00297.1
EMBL· GenBank· DDBJ
Genomic DNA
AL009126
EMBL· GenBank· DDBJ
CAB14954.1
EMBL· GenBank· DDBJ
Genomic DNA
CP052842
EMBL· GenBank· DDBJ
QJP89694.1
EMBL· GenBank· DDBJ
Genomic DNA
L31845
EMBL· GenBank· DDBJ
AAB40046.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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