CHI1_YERET
ID CHI1_YERET Reviewed; 542 AA.
AC B6A876;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Chitinase 1 {ECO:0000303|PubMed:21278295};
DE EC=3.2.1.14 {ECO:0000305|PubMed:22108167};
GN Name=chi1 {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 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 [3] {ECO:0007744|PDB:3OA5, ECO:0007744|PDB:4A5Q}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP 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).
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=580 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 6.0, 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; chi1
CC was not tested. {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; ABG33870.1; -; Genomic_DNA.
DR PDB; 3OA5; X-ray; 1.74 A; A/B=1-542.
DR PDB; 4A5Q; EM; 17.00 A; A/B/C/D/E=1-542.
DR PDBsum; 3OA5; -.
DR PDBsum; 4A5Q; -.
DR AlphaFoldDB; B6A876; -.
DR SMR; B6A876; -.
DR DIP; DIP-60375N; -.
DR IntAct; B6A876; 3.
DR STRING; 935293.PL78_03740; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EvolutionaryTrace; B6A876; -.
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..542
FT /note="Chitinase 1"
FT /id="PRO_0000445776"
FT DOMAIN 68..506
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 186..187
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 213..216
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 257
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 323..326
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 486
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 419..425
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:3OA5"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 465..478
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 494..502
FT /evidence="ECO:0007829|PDB:3OA5"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:3OA5"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:3OA5"
SQ SEQUENCE 542 AA; 60385 MW; 2F8B018D5B1D181C CRC64;
MEKEEKSNLI YDKDPGYVWD NKNECEGAAE ETYQELNYEP SISADKLTWT PTRLAKTVFN
TYEDDDDFNV LCYFTDWSQY DPRIINKEIR DTGGRSADIL RLNTPDGRPF KRLIYSFGGL
IGDKKYSADG NASIAVRLGV ATDPDDAIAN HKGKTIPVDP DGAVLASINC GFTKWEAGDA
NERYNQEKAK GLLGGFRLLH EADKELEFSL SIGGWSMSGL FSEIAKDEIL RTNFVEGIKD
FFQRFPMFSH LDIDWEYPGS IGAGNPNSPD DGANFAILIQ QITDAKISNL KGISIASSAD
PAKIDAANIP ALMDAGVTGI NLMTYDFFTL GDGKLSHHTN IYRDPSDVYS KYSIDDAVTH
LIDEKKVDPK AIFIGYAGYT RNAKNATITT SIPSEEALKG TYTDANQTLG SFEYSVLEWT
DIICHYMDFE KGEGRNGYKL VHDKVAKADY LYSEATKVFI SLDTPRSVRD KGRYVKDKGL
GGLFIWSGDQ DNGILTNAAH EGLKRRIKNK VIDMTPFYLD SDEELPTYTE PAEPQCEACN
IK
