CHI2_YERET
ID CHI2_YERET Reviewed; 633 AA.
AC B6A879;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Chitinase 2 {ECO:0000303|PubMed:21278295};
DE EC=3.2.1.14 {ECO:0000305|PubMed:22108167};
GN Name=chi2 {ECO:0000303|PubMed:21278295};
OS Yersinia entomophaga.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=935293;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-1678 / DSM 22339 / MH96;
RX PubMed=21278295; DOI=10.1128/jb.01044-10;
RA Hurst M.R., Jones S.A., Binglin T., Harper L.A., Jackson T.A., Glare T.R.;
RT "The main virulence determinant of Yersinia entomophaga MH96 is a broad-
RT host-range toxin complex active against insects.";
RL J. Bacteriol. 193:1966-1980(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-1678 / DSM 22339 / MH96;
RX PubMed=22108167; DOI=10.1016/j.jmb.2011.11.018;
RA Busby J.N., Landsberg M.J., Simpson R.M., Jones S.A., Hankamer B.,
RA Hurst M.R., Lott J.S.;
RT "Structural analysis of Chi1 chitinase from Yen-Tc: the multisubunit
RT insecticidal ABC toxin complex of Yersinia entomophaga.";
RL J. Mol. Biol. 415:359-371(2012).
RN [3]
RP ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF YEN-TC:K9 COMPLEX, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-1678 / DSM 22339 / MH96;
RX PubMed=22158901; DOI=10.1073/pnas.1111155108;
RA Landsberg M.J., Jones S.A., Rothnagel R., Busby J.N., Marshall S.D.,
RA Simpson R.M., Lott J.S., Hankamer B., Hurst M.R.;
RT "3D structure of the Yersinia entomophaga toxin complex and implications
RT for insecticidal activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20544-20549(2011).
RN [4] {ECO:0007744|PDB:4DWS}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 92-633.
RC STRAIN=ATCC BAA-1678 / DSM 22339 / MH96;
RX PubMed=23913273; DOI=10.1038/nature12465;
RA Busby J.N., Panjikar S., Landsberg M.J., Hurst M.R., Lott J.S.;
RT "The BC component of ABC toxins is an RHS-repeat-containing protein
RT encapsulation device.";
RL Nature 501:547-550(2013).
CC -!- FUNCTION: Part of an orally active toxin complex (TC) with strong
CC insecticidal effects on larvae of the Coleoptera Costelytra zealandica,
CC Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera
CC larvae (PubMed:21278295). The TC has an endochitinase activity
CC (PubMed:21278295, PubMed:22158901) (Probable). This subunit might aid
CC infection by degradation of the larval peritrophic membrane (Probable).
CC {ECO:0000269|PubMed:21278295, ECO:0000269|PubMed:22158901,
CC ECO:0000305|PubMed:22108167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000305|PubMed:22108167};
CC -!- ACTIVITY REGULATION: Toxin complex is secreted when grown at 25 degrees
CC Celsius or less; at higher temperatures the proteins are present
CC intracellularly but not secreted. {ECO:0000269|PubMed:21278295}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for 4-methylumbelliferyl-beta-D-N,N',N''-
CC triacetylchitotrioside {ECO:0000269|PubMed:22108167};
CC Note=In the intact toxin complex the combined chitinase activity of
CC Chi1 and Chi2 is slightly reduced. {ECO:0000269|PubMed:22108167};
CC pH dependence:
CC Optimum pH is 5.0, in the intact toxin complex optimum pH is pH 4.0
CC to pH 8.0. {ECO:0000269|PubMed:22108167};
CC -!- SUBUNIT: Semipurified toxin complex consists of at least YenA1-YenA2-
CC YenB-YenC1-YenC2-Chi1-Chi2 (PubMed:21278295). The Yen-TC:K9 subcomplex
CC is about 26 nm tall and 22 nm in diameter with 5-fold symmetry and 5
CC copies of YenA1, YenA2, Chi1 and Chi2; the chitinase subunits may be
CC solvent accessible on the exterior the complex (PubMed:22158901). The
CC Yen-TC:K9 subcomplex has no insecticidal activity (PubMed:22158901).
CC The native complex with additional YenB, YenC1 and YenC2 subunits is 16
CC nm taller and is insecticidal; the toxicity-conferring subunits are
CC present at about 1 copy each (PubMed:22158901).
CC {ECO:0000269|PubMed:21278295, ECO:0000269|PubMed:22158901}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21278295}.
CC Note=Secreted when grown at 25 degrees Celsius or less, but not when
CC grown at 30 or 37 degrees Celsius. {ECO:0000269|PubMed:21278295}.
CC -!- DISRUPTION PHENOTYPE: Cells with a disrupted yenA1-yenA2-chi2-yenB-
CC yenC1-yenC2 locus are no longer pathogenic in C.zealandica larvae.
CC {ECO:0000269|PubMed:21278295}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; DQ400808; ABG33867.1; -; Genomic_DNA.
DR RefSeq; WP_064513229.1; NZ_MWTM01000006.1.
DR PDB; 4DWS; X-ray; 1.80 A; A/B/C/D=92-633.
DR PDB; 6OGD; EM; 4.40 A; C/F/I/L/O=1-633.
DR PDBsum; 4DWS; -.
DR PDBsum; 6OGD; -.
DR AlphaFoldDB; B6A879; -.
DR SMR; B6A879; -.
DR DIP; DIP-60376N; -.
DR IntAct; B6A879; 1.
DR STRING; 935293.PL78_03755; -.
DR PATRIC; fig|935293.3.peg.808; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Virulence.
FT CHAIN 1..633
FT /note="Chitinase 2"
FT /id="PRO_0000445777"
FT DOMAIN 151..602
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 349
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 275..276
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 306..309
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 350
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 422..425
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 582
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 321..337
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 365..384
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 457..466
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 475..482
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 513..519
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:4DWS"
FT TURN 540..543
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 554..557
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 567..573
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 590..599
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 613..616
FT /evidence="ECO:0007829|PDB:4DWS"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:4DWS"
FT HELIX 627..631
FT /evidence="ECO:0007829|PDB:4DWS"
SQ SEQUENCE 633 AA; 69668 MW; E63D097BD2FE5D79 CRC64;
MVNKYTYTSS KAMSDISDVI GEPLAAWDSQ VGGRVFNVIF DGKVYTNTYW VERWQVPGIG
SSDGNPHNAW KFVRAATADE INKIGNPTTA DVKPTENIPS PILVEDKYTE ETYSRPDVNF
KEDGSQGNLS YTATRVCAPM YNHYVGDKTK PKLSAYITDW CQYDARLDGG GSKEEERGRG
FDLATLMQNP ATYDRLIFSF LGICGDIGNK SKKVQEVWDG WNAQAPSLGL PQIGKGHIVP
LDPYGDLGTA RNVGLPPESA DTSIESGTFL PYYQQNRAAG LLGGLRELQK KAHAMGHKLD
LAFSIGGWSL SSYFSALAEN PDERRVFVAS VVDFFVRFPM FSCVDIDWEY PGGGGDEGNI
SSDKDGENYV LLIKELRSAL DSRFGYSNRK EISIACSGVK AKLKKSNIDQ LVANGLDNIY
LMSYDFFGTI WADYIGHHTN LYSPKDPGEQ ELFDLSAEAA IDYLHNELGI PMEKIHLGYA
NYGRSAVGGD LTTRQYTKNG PALGTMENGA PEFFDIVKNY MDAEHSLSMG KNGFVLMTDT
NADADFLFSE AKGHFISLDT PRTVKQKGEY AAKNKLGGVF SWSGDQDCGL LANAAREGLG
YVADSNQETI DMGPLYNPGK EIYLKSISEI KSK
