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Endochitinase 42 (EC 3.2.1.14) (42 kDa endochitinase) (Chitinase 42)

 CHI42_TRIHA             Reviewed;         423 AA.
P48827;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
05-DEC-2018, entry version 94.
RecName: Full=Endochitinase 42;
EC=3.2.1.14;
AltName: Full=42 kDa endochitinase;
AltName: Full=Chitinase 42;
Flags: Precursor;
Name=chit42;
Trichoderma harzianum (Hypocrea lixii).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
Trichoderma.
NCBI_TaxID=5544;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 35-52; 93-107;
371-385 AND 397-414.
PubMed=7750151; DOI=10.1007/BF00326583;
Garcia I., Lora J.M., de la Cruz J., Benitez T., Llobell A.,
Pintor-Toro J.A.;
"Cloning and characterization of a chitinase (chit42) cDNA from the
mycoparasitic fungus Trichoderma harzianum.";
Curr. Genet. 27:83-89(1994).
[2]
INDUCTION, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=1606968; DOI=10.1111/j.1432-1033.1992.tb16994.x;
de la Cruz J., Hidalgo-Gallego A., Lora J.M., Benitez T.,
Pintor-Toro J.A., Llobell A.;
"Isolation and characterization of three chitinases from Trichoderma
harzianum.";
Eur. J. Biochem. 206:859-867(1992).
[3]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
STRAIN=T4;
PubMed=22744980; DOI=10.1002/pmic.201200048;
da Silva A.J., Gomez-Mendoza D.P., Junqueira M., Domont G.B.,
Ximenes Ferreira Filho E., de Sousa M.V., Ricart C.A.;
"Blue native-PAGE analysis of Trichoderma harzianum secretome reveals
cellulases and hemicellulases working as multienzymatic complexes.";
Proteomics 12:2729-2738(2012).
-!- FUNCTION: Secreted chitinase involved in the degradation of
chitin, a component of the cell walls of fungi and exoskeletal
elements of some animals (including worms and arthropods). Plays a
morphogenetic role during apical growth, cell division and
differentiation (cell wall morphogenesis). Acts also as an
antifungal agent. Involved in the degradation and further
assimilation of phytopathogenic fungi, namely mycoparasitism, the
major mechanism accounting for the antagonistic activity against
phytopathogenic fungi displayed by Trichoderma.
{ECO:0000269|PubMed:1606968}.
-!- CATALYTIC ACTIVITY:
Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
(1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
Evidence={ECO:0000269|PubMed:1606968};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.3 mg/ml for colloidal chitin {ECO:0000269|PubMed:1606968};
Temperature dependence:
Optimum temperature is 45-50 degrees Celsius.
{ECO:0000269|PubMed:1606968};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1606968,
ECO:0000269|PubMed:22744980}.
-!- INDUCTION: Specifically induced by chitin and is catabolite
repressed. {ECO:0000269|PubMed:1606968}.
-!- BIOTECHNOLOGY: The antagonistic activity of Trichoderma harzianum
is used for the control of several soil borne plant pathogenic
fungi.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
class V subfamily. {ECO:0000305}.
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EMBL; S78423; AAB34355.1; -; mRNA.
PIR; S51369; S51369.
PDB; 6EPB; X-ray; 1.75 A; A=1-423.
PDBsum; 6EPB; -.
ProteinModelPortal; P48827; -.
SMR; P48827; -.
CAZy; GH18; Glycoside Hydrolase Family 18.
mycoCLAP; CHI18D_TRIHA; -.
BRENDA; 3.2.1.14; 6445.
SABIO-RK; P48827; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.10.50.10; -; 1.
InterPro; IPR011583; Chitinase_II.
InterPro; IPR029070; Chitinase_insertion_sf.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR001579; Glyco_hydro_18_chit_AS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00704; Glyco_hydro_18; 1.
SMART; SM00636; Glyco_18; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF54556; SSF54556; 1.
PROSITE; PS01095; CHITINASE_18; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Chitin degradation;
Chitin-binding; Cleavage on pair of basic residues;
Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
Polysaccharide degradation; Secreted; Signal; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 34 {ECO:0000269|PubMed:7750151}.
/FTId=PRO_0000011934.
CHAIN 35 423 Endochitinase 42.
/FTId=PRO_0000011935.
ACT_SITE 171 171 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10053}.
CARBOHYD 218 218 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
STRAND 37 45 {ECO:0000244|PDB:6EPB}.
HELIX 46 49 {ECO:0000244|PDB:6EPB}.
HELIX 56 58 {ECO:0000244|PDB:6EPB}.
HELIX 61 63 {ECO:0000244|PDB:6EPB}.
STRAND 65 74 {ECO:0000244|PDB:6EPB}.
STRAND 80 83 {ECO:0000244|PDB:6EPB}.
HELIX 85 89 {ECO:0000244|PDB:6EPB}.
HELIX 107 118 {ECO:0000244|PDB:6EPB}.
STRAND 123 129 {ECO:0000244|PDB:6EPB}.
HELIX 137 140 {ECO:0000244|PDB:6EPB}.
HELIX 144 161 {ECO:0000244|PDB:6EPB}.
STRAND 164 169 {ECO:0000244|PDB:6EPB}.
HELIX 176 200 {ECO:0000244|PDB:6EPB}.
STRAND 207 213 {ECO:0000244|PDB:6EPB}.
HELIX 216 219 {ECO:0000244|PDB:6EPB}.
HELIX 224 230 {ECO:0000244|PDB:6EPB}.
STRAND 232 237 {ECO:0000244|PDB:6EPB}.
STRAND 246 248 {ECO:0000244|PDB:6EPB}.
HELIX 262 264 {ECO:0000244|PDB:6EPB}.
HELIX 269 278 {ECO:0000244|PDB:6EPB}.
HELIX 283 285 {ECO:0000244|PDB:6EPB}.
STRAND 286 297 {ECO:0000244|PDB:6EPB}.
STRAND 314 316 {ECO:0000244|PDB:6EPB}.
STRAND 319 321 {ECO:0000244|PDB:6EPB}.
HELIX 322 324 {ECO:0000244|PDB:6EPB}.
STRAND 331 335 {ECO:0000244|PDB:6EPB}.
TURN 336 339 {ECO:0000244|PDB:6EPB}.
STRAND 340 345 {ECO:0000244|PDB:6EPB}.
TURN 346 349 {ECO:0000244|PDB:6EPB}.
STRAND 350 353 {ECO:0000244|PDB:6EPB}.
HELIX 357 369 {ECO:0000244|PDB:6EPB}.
STRAND 374 378 {ECO:0000244|PDB:6EPB}.
HELIX 380 382 {ECO:0000244|PDB:6EPB}.
HELIX 386 388 {ECO:0000244|PDB:6EPB}.
HELIX 390 398 {ECO:0000244|PDB:6EPB}.
HELIX 416 419 {ECO:0000244|PDB:6EPB}.
TURN 420 422 {ECO:0000244|PDB:6EPB}.
SEQUENCE 423 AA; 46057 MW; DF90378EED1C30BE CRC64;
MLSFLGKSVA LLAALQATLS SPKPGHRRAS VEKRANGYAN SVYFTNWGIY DRNFQPADLV
ASDVTHVIYS FMNLQADGTV ISGDTYADYE KHYADDSWND VGTNAYGCVK QLFKVKKANR
GLKVLLSIGG WTWSTNFPSA ASTDANRKNF AKTAITFMKD WGFDGIDIDW EYPADATQAS
NMILLLKEVR SQRDAYAAQY APGYHFLLTI AAPAGKDNYS KLRLADLGQV LDYINLMAYD
YAGSFSPLTG HDANLFNNPS NPNATPFNTD SAVKDYINGG VPANKIVLGM PIYGRSFQNT
AGIGQTYNGV GSGSWEAGIW DYKALPKAGA TVQYDSVAKG YYSYNSATKE LISFDTPDMI
NTKVAYLKSL GLGGSMFWEA SADKKGADSV IGTSHRALGG LDTTQNLLSY PNSKYDNIKN
GLN


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