P17903 · RSBV_BACSU

Function

function

Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B.

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 Functionanti-sigma factor antagonist activity

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Anti-sigma-B factor antagonist
  • Alternative names
    • Anti-anti-sigma-B factor

Gene names

    • Name
      rsbV
    • Ordered locus names
      BSU04710

Organism names

Accessions

  • Primary accession
    P17903

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis56Loss of phosphorylation. Interacts strongly with RsbW.
Mutagenesis56No interaction with RsbW.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001941851-109Anti-sigma-B factor antagonist
Modified residue52Phosphoserine
Modified residue56Phosphoserine
Modified residue57Phosphothreonine

Post-translational modification

Phosphorylated by RsbW on a serine residue. Dephosphorylated by RsbP or RsbU.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Monomer (Probable). In stressed cells, forms a complex with RsbW. The predominant form of this complex has a stoichiometry of 2:2 (one dimer of RsbW is bound by two monomers of RsbV). Binds to RsbW in the presence of low levels of ATP or under conditions of energy or environmental stress (through dephosphorylation by RsbP or RsbU).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-109STAS

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    109
  • Mass (Da)
    11,939
  • Last updated
    1990-11-01 v1
  • Checksum
    12CB03E940463F2C
MNINVDVKQNENDIQVNIAGEIDVYSAPVLREKLVPLAEQGADLRICLKDVSYMDSTGLGVFVGTFKMVKKQGGSLKLENLSERLIRLFDITGLKDIIDISAKSEGGVQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M34995
EMBL· GenBank· DDBJ
AAA22711.1
EMBL· GenBank· DDBJ
Genomic DNA
L35574
EMBL· GenBank· DDBJ
AAA85084.1
EMBL· GenBank· DDBJ
Genomic DNA
AB001488
EMBL· GenBank· DDBJ
BAA19308.1
EMBL· GenBank· DDBJ
Genomic DNA
AL009126
EMBL· GenBank· DDBJ
CAB12278.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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