P06575 · BINA1_LYSSH
- ProteinBinary larvicide subunit BinA
- GenebinA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids370 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | toxin activity | |
Biological Process | sporulation resulting in formation of a cellular spore |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameBinary larvicide subunit BinA
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Lysinibacillus
Accessions
- Primary accessionP06575
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 22 | Decreased heterodimer solubility at pH 10, 10-20 fold less toxic to C.quinquefasciatus 4th instar larvae. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000448618 | 1-6 | ||||
Sequence: MRNLDF | ||||||
Chain | PRO_0000174111 | 7-370 | Binary larvicide subunit BinA | |||
Sequence: IDSFIPTEGKYIRVMDFYNSEYPFCIHAPSAPNGDIMTEICSRENNQYFIFFPTDDGRVIIANRHNGSVFTGEATSVVSDIYTGSPLQFFREVKRTMATYYLAIQNPESATDVRALEPHSHELPSRLYYTNNIENNSNILISNKEQIYLTLPSLPENEQYPKTPVLSGIDDIGPNQSEKSIIGSTLIPCIMVSDFISLGERMKTTPYYYVKHTQYWQSMWSALFPPGSKETKTEKSGITDTSQISMTDGINVSIGADFGLRFGNKTFGIKGGFTYDTKTQITNTSQLLIETTYTREYTNTENFPVRYTGYVLASEFTLHRSDGTQVNTIPWVALNDNYTTIARYPHFASEPLLGNTKIITDDQN | ||||||
Disulfide bond | 31↔47 | |||||
Sequence: CIHAPSAPNGDIMTEIC |
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
- PTM
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.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-155 | Beta-trefoil domain | ||||
Sequence: MRNLDFIDSFIPTEGKYIRVMDFYNSEYPFCIHAPSAPNGDIMTEICSRENNQYFIFFPTDDGRVIIANRHNGSVFTGEATSVVSDIYTGSPLQFFREVKRTMATYYLAIQNPESATDVRALEPHSHELPSRLYYTNNIENNSNILISNKEQIYL | ||||||
Region | 156-370 | Pore-forming domain | ||||
Sequence: TLPSLPENEQYPKTPVLSGIDDIGPNQSEKSIIGSTLIPCIMVSDFISLGERMKTTPYYYVKHTQYWQSMWSALFPPGSKETKTEKSGITDTSQISMTDGINVSIGADFGLRFGNKTFGIKGGFTYDTKTQITNTSQLLIETTYTREYTNTENFPVRYTGYVLASEFTLHRSDGTQVNTIPWVALNDNYTTIARYPHFASEPLLGNTKIITDDQN |
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)
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 statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length370
- Mass (Da)41,920
- Last updated1988-01-01 v1
- ChecksumBCB0D759A0D1B2D1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 31 | in Ref. 7; AA sequence | ||||
Sequence: C → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |