P0AFX9 · RSEB_ECOLI

Function

function

Negatively modulates the activity of sigma-E (RpoE) by stabilizing RseA under non-stress conditions. Although not essential for association of sigma-E with Rsea it increases their affinity 2- to 3-fold. When bound to RseA it prevents proteolysis by DegS, which is probably relieved by lipopolysaccharide binding (LPS).

Miscellaneous

Part of the rseD-rpoE-rseA-rseB-rseC operon (PubMed:28924029, PubMed:9159522, PubMed:9159523).

Activity regulation

Binding to RseA is inhibited by LPS fragments; phosphorylated N-acetylglucosamine (GlcNAc) with N-linked acyl chains are minimally necessary to disrupt binding to RseA. Once RseB is no longer bound to RseA the latter is susceptible to DegS degradation. Thus if periplasmic LPS levels increase the sigma-E regulon is induced.

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
Cellular Componentouter membrane-bounded periplasmic space
Cellular Componentplasma membrane
Cellular Componentsigma factor antagonist complex
Molecular Functionantisigma factor binding
Molecular Functionidentical protein binding
Molecular Functionlipid binding
Biological Processnegative regulation of DNA-templated transcription
Biological Processprotein stabilization
Biological Processregulation of polysaccharide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sigma-E factor regulatory protein RseB

Gene names

    • Name
      rseB
    • Ordered locus names
      b2571, JW2555

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MC1061 / ATCC 53338 / DSM 7140
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0AFX9
  • Secondary accessions
    • P46186
    • Q2MAF9

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

About 2-fold increased sigma-E activity, 2-fold decrease in stability of RseA.

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000002224924-318Sigma-E factor regulatory protein RseB

Proteomic databases

Interaction

Subunit

Homodimer. Interacts with RseA with 1:1 stoichiometry. Binding to LPS stabilzes a homotetramer that does not bind RseA.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P0AFX9rseA P0AFX79EBI-1135231, EBI-1117560
BINARY P0AFX9rseB P0AFX93EBI-1135231, EBI-1135231
View interactors in UniProtKB
View CPX-2532 in Complex Portal

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region24-203Responsible for oligomerization
Region222-318Interaction with RseA

Domain

The N-terminal domain (residues 24-203) is responsible for oligomerization, while the C-terminal domain (residues 222-318) interacts with RseA.

Sequence similarities

Belongs to the RseB family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    318
  • Mass (Da)
    35,750
  • Last updated
    2005-12-20 v1
  • Checksum
    3F8C34DD85600B54
MKQLWFAMSLVTGSLLFSANASATPASGALLQQMNLASQSLNYELSFISINKQGVESLRYRHARLDNRPLAQLLQMDGPRREVVQRGNEISYFEPGLEPFTLNGDYIVDSLPSLIYTDFKRLSPYYDFISVGRTRIADRLCEVIRVVARDGTRYSYIVWMDTESKLPMRVDLLDRDGETLEQFRVIAFNVNQDISSSMQTLAKANLPPLLSVPVGEKAKFSWTPTWLPQGFSEVSSSRRPLPTMDNMPIESRLYSDGLFSFSVNVNRATPSSTDQMLRTGRRTVSTSVRDNAEITIVGELPPQTAKRIAENIKFGAAQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U37089
EMBL· GenBank· DDBJ
AAC45316.1
EMBL· GenBank· DDBJ
Genomic DNA
U37455
EMBL· GenBank· DDBJ
AAC45319.1
EMBL· GenBank· DDBJ
Genomic DNA
D64044
EMBL· GenBank· DDBJ
BAA10918.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC75624.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE76747.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp