P10565 · BINB1_LYSSH
- ProteinBinary larvicide subunit BinB
- GenebinB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids448 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Component of a binary toxin active against Culex and some Aedes mosquito larvae (PubMed:8419297, Ref.6). This subunit alone has no toxic larvicidal activity (PubMed:3926751).
This subunit is responsible for localized binding to specific regions of the host larval gut. Binary toxin internalization into host gut cells requires both proteins (By similarity).
This subunit is responsible for localized binding to specific regions of the host larval gut. Binary toxin internalization into host gut cells requires both proteins (By similarity).
Miscellaneous
In protein gels runs as a 63 kDa protein.
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBinary larvicide subunit BinB
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Lysinibacillus
Accessions
- Primary accessionP10565
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000174114 | 1-448 | Binary larvicide subunit BinB | |||
Sequence: MCDSKDNSGVSEKCGKKFTNYPLNTTPTSLNYNLPEISKKFYNLKNKYSRNGYGLSKTEFPSSIENCPSNEYSIMYDNKDPRFLIRFLLDDGRYIIADRDDGEVFDEAPTYLDNNNHPIISRHYTGEERQKFEQVGSGDYITGEQFFQFYTQNKTRVLSNCRALDSRTILLSTAKIFPIYPPASETQLTAFVNSSFYAAAIPQLPQTSLLENIPEPTSLDDSGVLPKDAVRAVKGSALLPCIIVHDPNLNNSDKMKFNTYYLLEYKEYWHQLWSQIIPAHQTVKIQERTGISEVVQNSMIEDLNMYIGADFGMLFYFRSSGFKEQITRGLNRPLSQTTTQLGERVEEMEYYNSNDLDVRYVKYALAREFTLKRVNGEIVKNWVAVDYRLAGIQSYPNAPITNPLTLTKHTIIRCENSYDGHIFKTPLIFKNGEVIVKTNEELIPKINQ | ||||||
Disulfide bond | 67↔161 | |||||
Sequence: CPSNEYSIMYDNKDPRFLIRFLLDDGRYIIADRDDGEVFDEAPTYLDNNNHPIISRHYTGEERQKFEQVGSGDYITGEQFFQFYTQNKTRVLSNC |
Post-translational modification
Processed by proteases extracted from C.pipiens larval gut; unlike its partner BinA, it does not form a stable digestion product.
Keywords
- PTM
Expression
Developmental stage
Total crystal protein is produced during sporulation, it 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 BinA (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).
Interacts with mosquito protein Cpm1 which acts as its host receptor (PubMed:11483434).
Upon toxin crystal solubilization with NaOH at pH 12, only the 63-kDa (binB) and 43-kDa (binA) proteins were detected (PubMed:3926751).
Interacts with mosquito protein Cpm1 which acts as its host receptor (PubMed:11483434).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-198 | Beta-trefoil domain | ||||
Sequence: MCDSKDNSGVSEKCGKKFTNYPLNTTPTSLNYNLPEISKKFYNLKNKYSRNGYGLSKTEFPSSIENCPSNEYSIMYDNKDPRFLIRFLLDDGRYIIADRDDGEVFDEAPTYLDNNNHPIISRHYTGEERQKFEQVGSGDYITGEQFFQFYTQNKTRVLSNCRALDSRTILLSTAKIFPIYPPASETQLTAFVNSSFYA | ||||||
Region | 199-448 | Probable pore-forming domain | ||||
Sequence: AAIPQLPQTSLLENIPEPTSLDDSGVLPKDAVRAVKGSALLPCIIVHDPNLNNSDKMKFNTYYLLEYKEYWHQLWSQIIPAHQTVKIQERTGISEVVQNSMIEDLNMYIGADFGMLFYFRSSGFKEQITRGLNRPLSQTTTQLGERVEEMEYYNSNDLDVRYVKYALAREFTLKRVNGEIVKNWVAVDYRLAGIQSYPNAPITNPLTLTKHTIIRCENSYDGHIFKTPLIFKNGEVIVKTNEELIPKINQ |
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 possible 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
- Length448
- Mass (Da)51,431
- Last updated1989-07-01 v1
- Checksum55112D0131BCE018
Keywords
- Technical term