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CR1AA_BACTK
ID   CR1AA_BACTK             Reviewed;        1176 AA.
AC   P0A366; P02965; P09664; P09665; P16478; Q9RED5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Pesticidal crystal protein Cry1Aa;
DE   AltName: Full=133 kDa crystal protein;
DE   AltName: Full=Crystaline entomocidal protoxin;
DE   AltName: Full=Insecticidal delta-endotoxin CryIA(a);
GN   Name=cry1Aa; Synonyms=cry-1-1, cry1A(a), cryA, crybns3-1, cryIA(a), icp;
OS   Bacillus thuringiensis subsp. kurstaki.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=29339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HD-1;
RX   PubMed=2581950; DOI=10.1016/s0021-9258(18)88966-9;
RA   Schnepf H.E., Wong H.C., Whiteley H.R.;
RT   "The amino acid sequence of a crystal protein from Bacillus thuringiensis
RT   deduced from the DNA base sequence.";
RL   J. Biol. Chem. 260:6264-6272(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BNS3;
RA   Tounsi S., J'Mal A., Zouari N., Jaoua S.;
RT   "Cloning and nucleotide sequence of a novel cry1Aa-type gene from Bacillus
RT   thuringiensis subsp.kurstaki.";
RL   Biotechnol. Lett. 21:771-775(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-333, AND PROTEIN SEQUENCE OF 1-9.
RC   STRAIN=HD-1;
RX   PubMed=6296116; DOI=10.1016/s0021-9258(18)33082-5;
RA   Wong H.C., Schnepf H.E., Whiteley H.R.;
RT   "Transcriptional and translational start sites for the Bacillus
RT   thuringiensis crystal protein gene.";
RL   J. Biol. Chem. 258:1960-1967(1983).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 33-609.
RC   STRAIN=HD-1;
RX   PubMed=7490762; DOI=10.1006/jmbi.1995.0630;
RA   Grochulski P., Masson L., Borisova S., Pusztai-Carey M., Schwartz J.L.,
RA   Brousseau R., Cygler M.;
RT   "Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and
RT   channel formation.";
RL   J. Mol. Biol. 254:447-464(1995).
CC   -!- FUNCTION: Promotes colloidosmotic lysis by binding to the midgut
CC       epithelial cells of many lepidopteran larvae.
CC   -!- INTERACTION:
CC       P0A366; Q9XY09: btr175; Xeno; NbExp=10; IntAct=EBI-7210432, EBI-7210462;
CC   -!- DEVELOPMENTAL STAGE: The crystal protein is produced during sporulation
CC       and is accumulated both as an inclusion and as part of the spore coat.
CC   -!- MISCELLANEOUS: Toxic segment of the protein is located in the N-
CC       terminus.
CC   -!- SIMILARITY: Belongs to the delta endotoxin family. {ECO:0000305}.
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DR   EMBL; M11250; AAA22353.1; -; Genomic_DNA.
DR   EMBL; Y09663; CAA70856.1; -; mRNA.
DR   EMBL; J01554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A22617; A22617.
DR   PDB; 1CIY; X-ray; 2.25 A; A=29-618.
DR   PDBsum; 1CIY; -.
DR   AlphaFoldDB; P0A366; -.
DR   SMR; P0A366; -.
DR   IntAct; P0A366; 1.
DR   MINT; P0A366; -.
DR   EvolutionaryTrace; P0A366; -.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0001897; P:cytolysis by symbiont of host cells; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.190.10; -; 1.
DR   Gene3D; 2.100.10.10; -; 1.
DR   InterPro; IPR041587; Cry_V.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR038979; Pest_crys.
DR   InterPro; IPR005638; Pest_crys_C.
DR   InterPro; IPR005639; Pest_crys_N.
DR   InterPro; IPR036716; Pest_crys_N_sf.
DR   InterPro; IPR001178; Pest_cryst_cen_dom.
DR   InterPro; IPR036399; Pest_cryst_cen_dom_sf.
DR   PANTHER; PTHR37003; PTHR37003; 1.
DR   Pfam; PF17997; Cry1Ac_D5; 1.
DR   Pfam; PF03944; Endotoxin_C; 1.
DR   Pfam; PF00555; Endotoxin_M; 1.
DR   Pfam; PF03945; Endotoxin_N; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51096; SSF51096; 1.
DR   SUPFAM; SSF56849; SSF56849; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Sporulation; Toxin; Virulence.
FT   CHAIN           1..1176
FT                   /note="Pesticidal crystal protein Cry1Aa"
FT                   /id="PRO_0000174019"
FT   VARIANT         77
FT                   /note="P -> L (in strain: BNS3)"
FT   CONFLICT        1009
FT                   /note="V -> L (in Ref. 1; AAA22353)"
FT                   /evidence="ECO:0000305"
FT   HELIX           35..48
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           54..63
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           70..84
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           90..119
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           124..144
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           154..178
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           186..218
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           223..239
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           241..244
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           245..250
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   TURN            252..254
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          266..269
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           271..274
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           284..289
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          298..310
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          313..325
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           326..328
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          344..351
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          357..367
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          380..390
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          400..403
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          407..409
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           423..426
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          429..434
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          444..449
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          452..456
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          467..474
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           475..477
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          479..481
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          486..488
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          492..496
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          498..514
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          522..532
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          534..540
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          543..550
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   HELIX           562..564
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          566..569
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          577..590
FT                   /evidence="ECO:0007829|PDB:1CIY"
FT   STRAND          596..605
FT                   /evidence="ECO:0007829|PDB:1CIY"
SQ   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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