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Q06117 (CR3BB_BACTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pesticidal crystal protein cry3Bb
Alternative name(s):
74 kDa crystal protein
Crystaline entomocidal protoxin
Insecticidal delta-endotoxin CryIIIB(b)
Gene names
Name:cry3Bb
Synonyms:cryIIIB(b), cryIIIb2
OrganismBacillus thuringiensis
Taxonomic identifier1428 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. Has moderate level of toxicity to southern corn rootworm.

Subunit structure

Monomer.

Developmental stage

The crystal protein is produced during sporulation and is accumulated both as an inclusion and as part of the spore coat.

Miscellaneous

Toxic segment of the protein is located in the N-terminus.

Sequence similarities

Belongs to the delta endotoxin family.

Ontologies

Keywords
   Biological processSporulation
   Molecular functionToxin
   Technical term3D-structure
Gene Ontology (GO)
   Biological processdefense response

Inferred from electronic annotation. Source: InterPro

pathogenesis

Inferred from electronic annotation. Source: InterPro

sporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionreceptor binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Pesticidal crystal protein cry3Bb
PRO_0000174061

Natural variations

Natural variant211Q → P in strain: EG5144.
Natural variant971N → D in strain: EG5144.
Natural variant2891I → V in strain: EG5144.
Natural variant3521F → S in strain: EG5144.
Natural variant417 – 4193VYL → IYF in strain: EG5144.
Natural variant4511S → G in strain: EG5144.
Natural variant5901L → I in strain: EG5144.
Natural variant6001K → I in strain: EG5144.
Natural variant6241K → T in strain: EG5144.

Secondary structure

1 .......................................................................................... 652
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06117 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 63048332CDE8CCC6

FASTA65274,385
        10         20         30         40         50         60 
MNPNNRSEHD TIKVTPNSEL QTNHNQYPLA DNPNSTLEEL NYKEFLRMTE DSSTEVLDNS 

        70         80         90        100        110        120 
TVKDAVGTGI SVVGQILGVV GVPFAGALTS FYQSFLNTIW PSDADPWKAF MAQVEVLIDK 

       130        140        150        160        170        180 
KIEEYAKSKA LAELQGLQNN FEDYVNALNS WKKTPLSLRS KRSQDRIREL FSQAESHFRN 

       190        200        210        220        230        240 
SMPSFAVSKF EVLFLPTYAQ AANTHLLLLK DAQVFGEEWG YSSEDVAEFY HRQLKLTQQY 

       250        260        270        280        290        300 
TDHCVNWYNV GLNGLRGSTY DAWVKFNRFR REMTLTVLDL IVLFPFYDIR LYSKGVKTEL 

       310        320        330        340        350        360 
TRDIFTDPIF SLNTLQEYGP TFLSIENSIR KPHLFDYLQG IEFHTRLQPG YFGKDSFNYW 

       370        380        390        400        410        420 
SGNYVETRPS IGSSKTITSP FYGDKSTEPV QKLSFDGQKV YRTIANTDVA AWPNGKVYLG 

       430        440        450        460        470        480 
VTKVDFSQYD DQKNETSTQT YDSKRNNGHV SAQDSIDQLP PETTDEPLEK AYSHQLNYAE 

       490        500        510        520        530        540 
CFLMQDRRGT IPFFTWTHRS VDFFNTIDAE KITQLPVVKA YALSSGASII EGPGFTGGNL 

       550        560        570        580        590        600 
LFLKESSNSI AKFKVTLNSA ALLQRYRVRI RYASTTNLRL FVQNSNNDFL VIYINKTMNK 

       610        620        630        640        650 
DDDLTYQTFD LATTNSNMGF SGDKNELIIG AESFVSNEKI YIDKIEFIPV QL

« Hide

References

[1]"Characterization of two genes encoding Bacillus thuringiensis insecticidal crystal proteins toxic to Coleoptera species."
Donovan W.P., Rupar M.J., Slaney A.C., Malvar T., Gawron-Burke M.C., Johnson T.B.
Appl. Environ. Microbiol. 58:3921-3927(1992) [PubMed: 1476436] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: EG4961.
[2]"Bacillus thuringiensis cryIIIC, (b) protein toxic to coleopteran insects."
Donovan W.P., Rupar M.J., Slaney A.C.
Patent number US5378625, 03-JAN-1995
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NRRL B-18655 / EG5144.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M89794 Genomic DNA. Translation: AAA22334.1.
U31633 Genomic DNA. Translation: AAA74198.1.
PIRI39811.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JI6X-ray2.40A64-652[»]
ProteinModelPortalQ06117.
SMRQ06117. Positions 64-652.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005638. Endotoxin_C.
IPR001178. Endotoxin_cen_dom.
IPR015790. Endotoxin_cen_dom_subgr1.
IPR005639. Endotoxin_N.
IPR008979. Galactose-bd-like.
[Graphical view]
Gene3DG3DSA:2.100.10.10. Endotoxin_M. 1 hit.
G3DSA:1.20.190.10. Endotoxin_N. 1 hit.
PfamPF03944. Endotoxin_C. 1 hit.
PF00555. Endotoxin_M. 1 hit.
PF03945. Endotoxin_N. 1 hit.
[Graphical view]
SUPFAMSSF51096. Endotoxin. 1 hit.
SSF56849. Endotoxin_N. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCR3BB_BACTU
AccessionPrimary (citable) accession number: Q06117
Secondary accession number(s): Q45717
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 31, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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