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 27-MAR-2024, entry version 65. 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; Pseudomonadota; 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 CC 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside CC {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-20053; -. DR EMDB; EMD-20054; -. DR SMR; B6A879; -. DR DIP; DIP-60376N; -. DR IntAct; B6A879; 1. DR STRING; 935293.PL78_03755; -. DR PATRIC; fig|935293.3.peg.808; -. DR OrthoDB; 9775889at2; -. 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 Gene3D; 3.20.20.80; Glycosidases; 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 PANTHER; PTHR11177; CHITINASE; 1. DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1. DR Pfam; PF00704; Glyco_hydro_18; 1. DR SMART; SM00636; Glyco_18; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF54556; Chitinase insertion domain; 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 //