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Pesticidal crystal protein Cry1Aa (133 kDa crystal protein) (Crystaline entomocidal protoxin) (Insecticidal delta-endotoxin CryIA(a))

 CR1AA_BACTK             Reviewed;        1176 AA.
P0A366; P02965; P09664; P09665; P16478; Q9RED5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
18-JUL-2018, entry version 61.
RecName: Full=Pesticidal crystal protein Cry1Aa;
AltName: Full=133 kDa crystal protein;
AltName: Full=Crystaline entomocidal protoxin;
AltName: Full=Insecticidal delta-endotoxin CryIA(a);
Name=cry1Aa;
Synonyms=cry-1-1, cry1A(a), cryA, crybns3-1, cryIA(a), icp;
Bacillus thuringiensis subsp. kurstaki.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=29339;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=HD-1;
PubMed=2581950;
Schnepf H.E., Wong H.C., Whiteley H.R.;
"The amino acid sequence of a crystal protein from Bacillus
thuringiensis deduced from the DNA base sequence.";
J. Biol. Chem. 260:6264-6272(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BNS3;
Tounsi S., J'Mal A., Zouari N., Jaoua S.;
"Cloning and nucleotide sequence of a novel cry1Aa-type gene from
Bacillus thuringiensis subsp.kurstaki.";
Biotechnol. Lett. 21:771-775(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-333, AND PROTEIN SEQUENCE OF
1-9.
STRAIN=HD-1;
PubMed=6296116;
Wong H.C., Schnepf H.E., Whiteley H.R.;
"Transcriptional and translational start sites for the Bacillus
thuringiensis crystal protein gene.";
J. Biol. Chem. 258:1960-1967(1983).
[4]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 33-609.
STRAIN=HD-1;
PubMed=7490762; DOI=10.1006/jmbi.1995.0630;
Grochulski P., Masson L., Borisova S., Pusztai-Carey M.,
Schwartz J.L., Brousseau R., Cygler M.;
"Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure
and channel formation.";
J. Mol. Biol. 254:447-464(1995).
-!- FUNCTION: Promotes colloidosmotic lysis by binding to the midgut
epithelial cells of many lepidopteran larvae.
-!- INTERACTION:
Q9XY09:btr175 (xeno); NbExp=10; IntAct=EBI-7210432, EBI-7210462;
-!- 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.
-!- SIMILARITY: Belongs to the delta endotoxin family. {ECO:0000305}.
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EMBL; M11250; AAA22353.1; -; Genomic_DNA.
EMBL; Y09663; CAA70856.1; -; mRNA.
EMBL; J01554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A22617; A22617.
PDB; 1CIY; X-ray; 2.25 A; A=29-618.
PDBsum; 1CIY; -.
ProteinModelPortal; P0A366; -.
SMR; P0A366; -.
IntAct; P0A366; 1.
MINT; P0A366; -.
EvolutionaryTrace; P0A366; -.
GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
Gene3D; 1.20.190.10; -; 1.
Gene3D; 2.100.10.10; -; 1.
Gene3D; 2.60.120.260; -; 3.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR038979; Pest_crys.
InterPro; IPR005638; Pest_crys_C.
InterPro; IPR005639; Pest_crys_N.
InterPro; IPR036716; Pest_crys_N_sf.
InterPro; IPR001178; Pest_cryst_cen_dom.
InterPro; IPR036399; Pest_cryst_cen_dom_sf.
PANTHER; PTHR37003; PTHR37003; 1.
Pfam; PF03944; Endotoxin_C; 1.
Pfam; PF00555; Endotoxin_M; 1.
Pfam; PF03945; Endotoxin_N; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF51096; SSF51096; 1.
SUPFAM; SSF56849; SSF56849; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Sporulation; Toxin.
CHAIN 1 1176 Pesticidal crystal protein Cry1Aa.
/FTId=PRO_0000174019.
VARIANT 77 77 P -> L (in strain: BNS3).
CONFLICT 1009 1009 V -> L (in Ref. 1; AAA22353).
{ECO:0000305}.
HELIX 35 48 {ECO:0000244|PDB:1CIY}.
STRAND 51 53 {ECO:0000244|PDB:1CIY}.
HELIX 54 63 {ECO:0000244|PDB:1CIY}.
HELIX 70 84 {ECO:0000244|PDB:1CIY}.
HELIX 90 119 {ECO:0000244|PDB:1CIY}.
HELIX 124 144 {ECO:0000244|PDB:1CIY}.
HELIX 145 148 {ECO:0000244|PDB:1CIY}.
HELIX 154 178 {ECO:0000244|PDB:1CIY}.
HELIX 180 182 {ECO:0000244|PDB:1CIY}.
HELIX 186 218 {ECO:0000244|PDB:1CIY}.
HELIX 223 239 {ECO:0000244|PDB:1CIY}.
HELIX 241 244 {ECO:0000244|PDB:1CIY}.
HELIX 245 250 {ECO:0000244|PDB:1CIY}.
TURN 252 254 {ECO:0000244|PDB:1CIY}.
STRAND 266 269 {ECO:0000244|PDB:1CIY}.
HELIX 271 274 {ECO:0000244|PDB:1CIY}.
HELIX 284 289 {ECO:0000244|PDB:1CIY}.
STRAND 298 310 {ECO:0000244|PDB:1CIY}.
STRAND 313 325 {ECO:0000244|PDB:1CIY}.
HELIX 326 328 {ECO:0000244|PDB:1CIY}.
STRAND 344 351 {ECO:0000244|PDB:1CIY}.
STRAND 357 367 {ECO:0000244|PDB:1CIY}.
STRAND 380 390 {ECO:0000244|PDB:1CIY}.
STRAND 393 395 {ECO:0000244|PDB:1CIY}.
STRAND 400 403 {ECO:0000244|PDB:1CIY}.
STRAND 407 409 {ECO:0000244|PDB:1CIY}.
HELIX 410 412 {ECO:0000244|PDB:1CIY}.
HELIX 423 426 {ECO:0000244|PDB:1CIY}.
STRAND 429 434 {ECO:0000244|PDB:1CIY}.
STRAND 444 449 {ECO:0000244|PDB:1CIY}.
STRAND 452 456 {ECO:0000244|PDB:1CIY}.
STRAND 467 474 {ECO:0000244|PDB:1CIY}.
HELIX 475 477 {ECO:0000244|PDB:1CIY}.
STRAND 479 481 {ECO:0000244|PDB:1CIY}.
STRAND 486 488 {ECO:0000244|PDB:1CIY}.
STRAND 492 496 {ECO:0000244|PDB:1CIY}.
STRAND 498 514 {ECO:0000244|PDB:1CIY}.
STRAND 522 532 {ECO:0000244|PDB:1CIY}.
STRAND 534 540 {ECO:0000244|PDB:1CIY}.
STRAND 543 550 {ECO:0000244|PDB:1CIY}.
HELIX 562 564 {ECO:0000244|PDB:1CIY}.
STRAND 566 569 {ECO:0000244|PDB:1CIY}.
STRAND 577 590 {ECO:0000244|PDB:1CIY}.
STRAND 596 605 {ECO:0000244|PDB:1CIY}.
SEQUENCE 1176 AA; 133120 MW; E2EE15AF12E5DD85 CRC64;
MDNNPNINEC IPYNCLSNPE VEVLGGERIE TGYTPIDISL SLTQFLLSEF VPGAGFVLGL
VDIIWGIFGP SQWDAFPVQI EQLINQRIEE FARNQAISRL EGLSNLYQIY AESFREWEAD
PTNPALREEM RIQFNDMNSA LTTAIPLLAV QNYQVPLLSV YVQAANLHLS VLRDVSVFGQ
RWGFDAATIN SRYNDLTRLI GNYTDYAVRW YNTGLERVWG PDSRDWVRYN QFRRELTLTV
LDIVALFSNY DSRRYPIRTV SQLTREIYTN PVLENFDGSF RGMAQRIEQN IRQPHLMDIL
NSITIYTDVH RGFNYWSGHQ ITASPVGFSG PEFAFPLFGN AGNAAPPVLV SLTGLGIFRT
LSSPLYRRII LGSGPNNQEL FVLDGTEFSF ASLTTNLPST IYRQRGTVDS LDVIPPQDNS
VPPRAGFSHR LSHVTMLSQA AGAVYTLRAP TFSWQHRSAE FNNIIPSSQI TQIPLTKSTN
LGSGTSVVKG PGFTGGDILR RTSPGQISTL RVNITAPLSQ RYRVRIRYAS TTNLQFHTSI
DGRPINQGNF SATMSSGSNL QSGSFRTVGF TTPFNFSNGS SVFTLSAHVF NSGNEVYIDR
IEFVPAEVTF EAEYDLERAQ KAVNELFTSS NQIGLKTDVT DYHIDQVSNL VECLSDEFCL
DEKQELSEKV KHAKRLSDER NLLQDPNFRG INRQLDRGWR GSTDITIQGG DDVFKENYVT
LLGTFDECYP TYLYQKIDES KLKAYTRYQL RGYIEDSQDL EIYLIRYNAK HETVNVPGTG
SLWPLSAQSP IGKCGEPNRC APHLEWNPDL DCSCRDGEKC AHHSHHFSLD IDVGCTDLNE
DLGVWVIFKI KTQDGHARLG NLEFLEEKPL VGEALARVKR AEKKWRDKRE KLEWETNIVY
KEAKESVDAL FVNSQYDQLQ ADTNIAMIHA ADKRVHSIRE AYLPELSVIP GVNAAIFEEL
EGRIFTAFSL YDARNVIKNG DFNNGLSCWN VKGHVDVEEQ NNQRSVLVVP EWEAEVSQEV
RVCPGRGYIL RVTAYKEGYG EGCVTIHEIE NNTDELKFSN CVEEEIYPNN TVTCNDYTVN
QEEYGGAYTS RNRGYNEAPS VPADYASVYE EKSYTDGRRE NPCEFNRGYR DYTPLPVGYV
TKELEYFPET DKVWIEIGET EGTFIVDSVE LLLMEE


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MSK-2 Crystal Harvesting Sampler Kit, contains 100 mounts for crystal harvesting and data collection; 20 Dual Thickness MicroMounts, 20 MicroLoops LD, 20 MicroMesh, 20 MicroLoop E, and 20 MicroGrippers kit
MSK-2 Crystal Harvesting Sampler Kit, contains 100 mounts for crystal harvesting and data collection; 20 Dual Thickness MicroMounts, 20 MicroLoops LD, 20 MicroMesh, 20 MicroLoop E, and 20 MicroGrippers 1 kit
MSK-2 Crystal Harvesting Sampler Kit, contains 100 mounts for crystal harvesting and data collection; 20 Dual Thickness MicroMounts, 20 MicroLoops LD, 20 MicroMesh, 20 MicroLoop E, and 20 MicroGrippers kit
MSK-1 Crystal Harvesting Sampler Kit, contains 40 mounts for crystal harvesting and data collection; 10 Dual Thickness MicroMounts, 10 MicroLoops, 5 MicroMesh, 5 MicroLoop LD, 5 MicroLoop E, and 5 MicroGrip 1 kit
MSK-1 Crystal Harvesting Sampler Kit, contains 40 mounts for crystal harvesting and data collection; 10 Dual Thickness MicroMounts, 10 MicroLoops, 5 MicroMesh, 5 MicroLoop LD, 5 MicroLoop E, and 5 MicroGrip kit
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