P06575 · BINA1_LYSSH

Function

function

Component of a binary toxin active against Culex and some Aedes mosquito larvae; about 1000-fold more toxic against C.quinquefasciatus than A.aegypti (Probable) (PubMed:8419297, Ref.10). This subunit alone is active against C.quinquefasciatus, Anopheles gambiae, A.stephensi and Aedes aegypti mosquito cell lines; non Culex mosquitoes are less sensitive to the toxin (Probable) (PubMed:2886104).
Binary toxin internalization into host gut cells requires both proteins (By similarity).

Activity regulation

Toxic activity of the cleaved 40 kDa form of this subunit alone on cells of C.quinquefasciatus is decreased about 50% by chitobiose, chitotriose, N-acetylmuramic acid and N-acetylneuraminic acid.

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 Functiontoxin activity
Biological Processsporulation resulting in formation of a cellular spore

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Binary larvicide subunit BinA
  • Alternative names
    • 41.9 kDa insecticidal toxin
    • Binary paracrystalline larvicide subunit BinA

Gene names

    • Name
      binA

Organism names

Accessions

  • Primary accession
    P06575

Subcellular Location

Spore, perispore

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis22Decreased heterodimer solubility at pH 10, 10-20 fold less toxic to C.quinquefasciatus 4th instar larvae.

PTM/Processing

Features

Showing features for propeptide, chain, disulfide bond.

TypeIDPosition(s)Description
PropeptidePRO_00004486181-6
ChainPRO_00001741117-370Binary larvicide subunit BinA
Disulfide bond31↔47

Post-translational modification

Processed by proteases extracted from C.pipiens larval gut; 6 amino acids are removed from the N-terminus while it is estimated about 20 residues are removed from the C-terminus to yield the 40 kDa toxin form that is seen in insects. The 40 kDa form is 50-fold more lethal against tissue culture cells than the precursor form. Larval gut extracts of Aedes aegypti and Anopheles gambiae also generate the same 40 kDa form all of which are toxic in C.pipiens.

Keywords

Expression

Developmental stage

Total crystal protein is produced during sporulation, appears after 6 hours of growth, and represents about 4.8% of cellular dry weight in stationary phase. It probably accumulates next to spores within the exosporeum.

Interaction

Subunit

Forms a heterodimer with BinB (PubMed:27680699).
Upon toxin crystal solubilization with NaOH at pH 12, only the 63-kDa (binB) and 43-kDa (binA) proteins were detected (PubMed:3926751).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-155Beta-trefoil domain
Region156-370Pore-forming domain

Domain

Has an N-terminal beta-trefoil domain and a C-terminal pore-forming domain. The trefoil domain has barrel and cap subdomains; the cap has 3 carbohydrate-binding modules while the barrel is involved in host cell receptor binding. At neutral pH the carbohydrate-binding modules are accessible on the toxin surface but the barrel subdomain is not (PubMed:27680699).
The crystal is very stable at neutral pH, upon ingestion by larvae the crystals dissolve in the alkaline midgut. As the pH rises the 2 subunits compact, while deprotonation at up to 4 sites (including the N- and C-termini) increases the accessibility of the propeptides and moves subdomains. The combined pH-induced changes are thought to expose the previously hidden receptor-binding motif and lead to crystal dissolution (Probable)

Sequence similarities

Belongs to the toxin_10 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    370
  • Mass (Da)
    41,920
  • Last updated
    1988-01-01 v1
  • Checksum
    BCB0D759A0D1B2D1
MRNLDFIDSFIPTEGKYIRVMDFYNSEYPFCIHAPSAPNGDIMTEICSRENNQYFIFFPTDDGRVIIANRHNGSVFTGEATSVVSDIYTGSPLQFFREVKRTMATYYLAIQNPESATDVRALEPHSHELPSRLYYTNNIENNSNILISNKEQIYLTLPSLPENEQYPKTPVLSGIDDIGPNQSEKSIIGSTLIPCIMVSDFISLGERMKTTPYYYVKHTQYWQSMWSALFPPGSKETKTEKSGITDTSQISMTDGINVSIGADFGLRFGNKTFGIKGGFTYDTKTQITNTSQLLIETTYTREYTNTENFPVRYTGYVLASEFTLHRSDGTQVNTIPWVALNDNYTTIARYPHFASEPLLGNTKIITDDQN

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict31in Ref. 7; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y00378
EMBL· GenBank· DDBJ
CAA68450.1
EMBL· GenBank· DDBJ
Genomic DNA
M20390
EMBL· GenBank· DDBJ
AAA22861.1
EMBL· GenBank· DDBJ
Genomic DNA
M36957
EMBL· GenBank· DDBJ
AAA22862.1
EMBL· GenBank· DDBJ
mRNA
AJ224477
EMBL· GenBank· DDBJ
CAB37655.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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