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P0A366

- CR1AA_BACTK

UniProt

P0A366 - CR1AA_BACTK

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Protein

Pesticidal crystal protein cry1Aa

Gene
cry1Aa, cry-1-1, cry1A(a), cryA, crybns3-1, cryIA(a), icp
Organism
Bacillus thuringiensis subsp. kurstaki
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae.

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. defense response Source: InterPro
  2. pathogenesis Source: InterPro
  3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Biological processi

Sporulation

Names & Taxonomyi

Protein namesi
Recommended name:
Pesticidal crystal protein cry1Aa
Alternative name(s):
133 kDa crystal protein
Crystaline entomocidal protoxin
Insecticidal delta-endotoxin CryIA(a)
Gene namesi
Name:cry1Aa
Synonyms:cry-1-1, cry1A(a), cryA, crybns3-1, cryIA(a), icp
OrganismiBacillus thuringiensis subsp. kurstaki
Taxonomic identifieri29339 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11761176Pesticidal crystal protein cry1AaPRO_0000174019Add
BLAST

Expressioni

Developmental stagei

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

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
btr175Q9XY0910EBI-7210432,EBI-7210462From a different organism.

Protein-protein interaction databases

IntActiP0A366. 1 interaction.
MINTiMINT-7259645.

Structurei

Secondary structure

1
1176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 4814
Beta strandi51 – 533
Helixi54 – 6310
Helixi70 – 8415
Helixi90 – 11930
Helixi124 – 14421
Helixi145 – 1484
Helixi154 – 17825
Helixi180 – 1823
Helixi186 – 21833
Helixi223 – 23917
Helixi241 – 2444
Helixi245 – 2506
Turni252 – 2543
Beta strandi266 – 2694
Helixi271 – 2744
Helixi284 – 2896
Beta strandi298 – 31013
Beta strandi313 – 32513
Helixi326 – 3283
Beta strandi344 – 3518
Beta strandi357 – 36711
Beta strandi380 – 39011
Beta strandi393 – 3953
Beta strandi400 – 4034
Beta strandi407 – 4093
Helixi410 – 4123
Helixi423 – 4264
Beta strandi429 – 4346
Beta strandi444 – 4496
Beta strandi452 – 4565
Beta strandi467 – 4748
Helixi475 – 4773
Beta strandi479 – 4813
Beta strandi486 – 4883
Beta strandi492 – 4965
Beta strandi498 – 51417
Beta strandi522 – 53211
Beta strandi534 – 5407
Beta strandi543 – 5508
Helixi562 – 5643
Beta strandi566 – 5694
Beta strandi577 – 59014
Beta strandi596 – 60510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIYX-ray2.25A29-618[»]
ProteinModelPortaliP0A366.
SMRiP0A366. Positions 33-609.

Miscellaneous databases

EvolutionaryTraceiP0A366.

Family & Domainsi

Sequence similaritiesi

Belongs to the delta endotoxin family.

Family and domain databases

Gene3Di1.20.190.10. 1 hit.
2.100.10.10. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR005638. Endotoxin_C.
IPR001178. Endotoxin_cen_dom.
IPR015790. Endotoxin_cen_dom_subgr1.
IPR005639. Endotoxin_N.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF03944. Endotoxin_C. 1 hit.
PF00555. Endotoxin_M. 1 hit.
PF03945. Endotoxin_N. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51096. SSF51096. 1 hit.
SSF56849. SSF56849. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A366-1 [UniParc]FASTAAdd to Basket

« Hide

MDNNPNINEC IPYNCLSNPE VEVLGGERIE TGYTPIDISL SLTQFLLSEF     50
VPGAGFVLGL VDIIWGIFGP SQWDAFPVQI EQLINQRIEE FARNQAISRL 100
EGLSNLYQIY AESFREWEAD PTNPALREEM RIQFNDMNSA LTTAIPLLAV 150
QNYQVPLLSV YVQAANLHLS VLRDVSVFGQ RWGFDAATIN SRYNDLTRLI 200
GNYTDYAVRW YNTGLERVWG PDSRDWVRYN QFRRELTLTV LDIVALFSNY 250
DSRRYPIRTV SQLTREIYTN PVLENFDGSF RGMAQRIEQN IRQPHLMDIL 300
NSITIYTDVH RGFNYWSGHQ ITASPVGFSG PEFAFPLFGN AGNAAPPVLV 350
SLTGLGIFRT LSSPLYRRII LGSGPNNQEL FVLDGTEFSF ASLTTNLPST 400
IYRQRGTVDS LDVIPPQDNS VPPRAGFSHR LSHVTMLSQA AGAVYTLRAP 450
TFSWQHRSAE FNNIIPSSQI TQIPLTKSTN LGSGTSVVKG PGFTGGDILR 500
RTSPGQISTL RVNITAPLSQ RYRVRIRYAS TTNLQFHTSI DGRPINQGNF 550
SATMSSGSNL QSGSFRTVGF TTPFNFSNGS SVFTLSAHVF NSGNEVYIDR 600
IEFVPAEVTF EAEYDLERAQ KAVNELFTSS NQIGLKTDVT DYHIDQVSNL 650
VECLSDEFCL DEKQELSEKV KHAKRLSDER NLLQDPNFRG INRQLDRGWR 700
GSTDITIQGG DDVFKENYVT LLGTFDECYP TYLYQKIDES KLKAYTRYQL 750
RGYIEDSQDL EIYLIRYNAK HETVNVPGTG SLWPLSAQSP IGKCGEPNRC 800
APHLEWNPDL DCSCRDGEKC AHHSHHFSLD IDVGCTDLNE DLGVWVIFKI 850
KTQDGHARLG NLEFLEEKPL VGEALARVKR AEKKWRDKRE KLEWETNIVY 900
KEAKESVDAL FVNSQYDQLQ ADTNIAMIHA ADKRVHSIRE AYLPELSVIP 950
GVNAAIFEEL EGRIFTAFSL YDARNVIKNG DFNNGLSCWN VKGHVDVEEQ 1000
NNQRSVLVVP EWEAEVSQEV RVCPGRGYIL RVTAYKEGYG EGCVTIHEIE 1050
NNTDELKFSN CVEEEIYPNN TVTCNDYTVN QEEYGGAYTS RNRGYNEAPS 1100
VPADYASVYE EKSYTDGRRE NPCEFNRGYR DYTPLPVGYV TKELEYFPET 1150
DKVWIEIGET EGTFIVDSVE LLLMEE 1176
Length:1,176
Mass (Da):133,120
Last modified:March 15, 2005 - v1
Checksum:iE2EE15AF12E5DD85
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771P → L in strain: BNS3.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1009 – 10091V → L in AAA22353. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11250 Genomic DNA. Translation: AAA22353.1.
Y09663 mRNA. Translation: CAA70856.1.
J01554 Genomic DNA. No translation available.
PIRiA22617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11250 Genomic DNA. Translation: AAA22353.1 .
Y09663 mRNA. Translation: CAA70856.1 .
J01554 Genomic DNA. No translation available.
PIRi A22617.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CIY X-ray 2.25 A 29-618 [» ]
ProteinModelPortali P0A366.
SMRi P0A366. Positions 33-609.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A366. 1 interaction.
MINTi MINT-7259645.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0A366.

Family and domain databases

Gene3Di 1.20.190.10. 1 hit.
2.100.10.10. 1 hit.
2.60.120.260. 1 hit.
InterProi IPR005638. Endotoxin_C.
IPR001178. Endotoxin_cen_dom.
IPR015790. Endotoxin_cen_dom_subgr1.
IPR005639. Endotoxin_N.
IPR008979. Galactose-bd-like.
[Graphical view ]
Pfami PF03944. Endotoxin_C. 1 hit.
PF00555. Endotoxin_M. 1 hit.
PF03945. Endotoxin_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF51096. SSF51096. 1 hit.
SSF56849. SSF56849. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The amino acid sequence of a crystal protein from Bacillus thuringiensis deduced from the DNA base sequence."
    Schnepf H.E., Wong H.C., Whiteley H.R.
    J. Biol. Chem. 260:6264-6272(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: HD-1-Dippel.
  2. "Cloning and nucleotide sequence of a novel cry1Aa-type gene from Bacillus thuringiensis subsp.kurstaki."
    Tounsi S., J'Mal A., Zouari N., Jaoua S.
    Biotechnol. Lett. 21:771-775(1999)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BNS3.
  3. "Transcriptional and translational start sites for the Bacillus thuringiensis crystal protein gene."
    Wong H.C., Schnepf H.E., Whiteley H.R.
    J. Biol. Chem. 258:1960-1967(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-333, PROTEIN SEQUENCE OF 1-9.
    Strain: HD-1-Dippel.
  4. "Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation."
    Grochulski P., Masson L., Borisova S., Pusztai-Carey M., Schwartz J.L., Brousseau R., Cygler M.
    J. Mol. Biol. 254:447-464(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 33-609.
    Strain: HD-1-Dippel.

Entry informationi

Entry nameiCR1AA_BACTK
AccessioniPrimary (citable) accession number: P0A366
Secondary accession number(s): P02965
, P09664, P09665, P16478, Q9RED5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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