CR4AA_BACTI
ID CR4AA_BACTI Reviewed; 1180 AA.
AC P16480;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Pesticidal crystal protein Cry4Aa;
DE AltName: Full=135 kDa crystal protein;
DE AltName: Full=Crystaline entomocidal protoxin;
DE AltName: Full=Insecticidal delta-endotoxin CryIVA(a);
GN Name=cry4Aa; Synonyms=cryIVA(a), isrH4;
OS Bacillus thuringiensis subsp. israelensis.
OG Plasmid 72 Kb.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sen K., Honda G., Koyama N., Nishida M., Neki A., Sakai H., Himeno M.,
RA Komano T.;
RT "Cloning and nucleotide sequences of the two 130 kDa insecticidal protein
RT genes of Bacillus thuringiensis var. israelensis.";
RL Agric. Biol. Chem. 52:873-878(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2821500; DOI=10.1093/nar/15.17.7195;
RA Ward E.S., Ellar D.J.;
RT "Nucleotide sequence of a Bacillus thuringiensis var. israelensis gene
RT encoding a 130 kDa delta-endotoxin.";
RL Nucleic Acids Res. 15:7195-7195(1987).
RN [3]
RP MUTAGENESIS.
RX PubMed=7913448; DOI=10.1016/0014-5793(94)00604-0;
RA Nishimoto T., Yoshisue H., Ihara K., Sakai H., Komano T.;
RT "Functional analysis of block 5, one of the highly conserved amino acid
RT sequences in the 130-kDa CryIVA protein produced by Bacillus thuringiensis
RT subsp. israelensis.";
RL FEBS Lett. 348:249-254(1994).
CC -!- FUNCTION: Promotes colloidosmotic lysis by binding to the midgut
CC epithelial cells of insects.
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 -!- MISCELLANEOUS: Diverse amino acid mutations in sequence block 667-676
CC have no direct effect on the insecticidal activity but alter the
CC structural stability of the toxin protein molecule.
CC -!- SIMILARITY: Belongs to the delta endotoxin family. {ECO:0000305}.
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DR EMBL; D00248; BAA00179.1; -; Genomic_DNA.
DR EMBL; Y00423; CAA68485.1; -; Genomic_DNA.
DR PIR; A26858; A26858.
DR PIR; I39870; I39870.
DR RefSeq; WP_012211114.1; NZ_LC128536.1.
DR RefSeq; YP_001573833.1; NC_010076.1.
DR PDB; 2C9K; X-ray; 2.80 A; A=68-679.
DR PDBsum; 2C9K; -.
DR AlphaFoldDB; P16480; -.
DR SMR; P16480; -.
DR EvolutionaryTrace; P16480; -.
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; 2.
DR SUPFAM; SSF51096; SSF51096; 1.
DR SUPFAM; SSF56849; SSF56849; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Plasmid; Sporulation; Toxin; Virulence.
FT CHAIN 1..1180
FT /note="Pesticidal crystal protein Cry4Aa"
FT /id="PRO_0000174063"
FT CONFLICT 306
FT /note="L -> V (in Ref. 2; CAA68485)"
FT /evidence="ECO:0000305"
FT CONFLICT 1052
FT /note="T -> I (in Ref. 2; CAA68485)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="R -> G (in Ref. 2; CAA68485)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127
FT /note="C -> W (in Ref. 2; CAA68485)"
FT /evidence="ECO:0000305"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:2C9K"
FT TURN 89..95
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:2C9K"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:2C9K"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 170..190
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 207..231
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 250..275
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:2C9K"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 380..389
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 450..463
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 498..507
FT /evidence="ECO:0007829|PDB:2C9K"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 517..524
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 570..579
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 584..594
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 603..608
FT /evidence="ECO:0007829|PDB:2C9K"
FT TURN 609..611
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:2C9K"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 651..658
FT /evidence="ECO:0007829|PDB:2C9K"
FT STRAND 667..676
FT /evidence="ECO:0007829|PDB:2C9K"
SQ SEQUENCE 1180 AA; 134539 MW; 6FB5B6979DACAD3B CRC64;
MNPYQNKNEY ETLNASQKKL NISNNYTRYP IENSPKQLLQ STNYKDWLNM CQQNQQYGGD
FETFIDSGEL SAYTIVVGTV LTGFGFTTPL GLALIGFGTL IPVLFPAQDQ SNTWSDFITQ
TKNIIKKEIA STYISNANKI LNRSFNVIST YHNHLKTWEN NPNPQNTQDV RTQIQLVHYH
FQNVIPELVN SCPPNPSDCD YYNILVLSSY AQAANLHLTV LNQAVKFEAY LKNNRQFDYL
EPLPTAIDYY PVLTKAIEDY TNYCVTTYKK GLNLIKTTPD SNLDGNINWN TYNTYRTKMT
TAVLDLVALF PNYDVGKYPI GVQSELTREI YQVLNFEESP YKYYDFQYQE DSLTRRPHLF
TWLDSLNFYE KAQTTPNNFF TSHYNMFHYT LDNISQKSSV FGNHNVTDKL KSLGLATNIY
IFLLNVISLD NKYLNDYNNI SKMDFFITNG TRLLEKELTA GSGQITYDVN KNIFGLPILK
RRENQGNPTL FPTYDNYSHI LSFIKSLSIP ATYKTQVYTF AWTHSSVDPK NTIYTHLTTQ
IPAVKANSLG TASKVVQGPG HTGGDLIDFK DHFKITCQHS NFQQSYFIRI RYASNGSANT
RAVINLSIPG VAELGMALNP TFSGTDYTNL KYKDFQYLEF SNEVKFAPNQ NISLVFNRSD
VYTNTTVLID KIEFLPITRS IREDREKQKL ETVQQIINTF YANPIKNTLQ SELTDYDIDQ
AANLVECISE ELYPKEKMLL LDEVKNAKQL SQSRNVLQNG DFESATLGWT TSDNITIQED
DPIFKGHYLH MSGARDIDGT IFPTYIFQKI DESKLKPYTR YLVRGFVGSS KDVELVVSRY
GEEIDAIMNV PADLNYLYPS TFDCEGSNRC ETSAVPANIG NTSDMLYSCQ YDTGKKHVVC
QDSHQFSFTI DTGALDTNEN IGVWVMFKIS SPDGYASLDN LEVIEEGPID GEALSRVKHM
EKKWNDQMEA KRSETQQAYD VAKQAIDALF TNVQDEALQF DTTLAQIQYA EYLVQSIPYV
YNDWLSDVPG MNYDIYVELD ARVAQARYLY DTRNIIKNGD FTQGVMGWHV TGNADVQQID
GVSVLVLSNW SAGVSQNVHL QHNHGYVLRV IAKKEGPGNG YVTLMDCEEN QEKLTFTSCE
EGYITKTVDV FPDTDRVRIE IGETEGSFYI ESIELICMNE
