CHIQ_TOBAC
ID CHIQ_TOBAC Reviewed; 253 AA.
AC P17514;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Acidic endochitinase Q;
DE EC=3.2.1.14;
DE AltName: Full=Pathogenesis-related protein Q;
DE Short=PR-Q;
DE Flags: Precursor;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Xanthi NC;
RX PubMed=2296608; DOI=10.1073/pnas.87.1.98;
RA Payne G., Ahl P., Moyer M., Harper A., Beck J., Meins F. Jr., Ryals J.;
RT "Isolation of complementary DNA clones encoding pathogenesis-related
RT proteins P and Q, two acidic chitinases from tobacco.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:98-102(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun; TISSUE=Leaf;
RX PubMed=2131096; DOI=10.1094/mpmi-3-252;
RA Linthorst H.J.M., van Loon L.C., van Rossum C.M.A., Mayer A., Bol J.F.,
RA van Roekel J., Meulenhof J., Conelissen B.J.C.;
RT "Analysis of acidic and basic chitinases from tobacco and petunia and their
RT constitutive expression in transgenic tobacco.";
RL Mol. Plant Microbe Interact. 3:252-258(1990).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens.
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 -!- SUBCELLULAR LOCATION: Secreted. Note=Extracellular fluid from leaves.
CC -!- INDUCTION: By TMV infection.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; M29868; AAA34107.1; -; mRNA.
DR EMBL; X51425; CAA35789.1; -; mRNA.
DR PIR; B34801; B34801.
DR PIR; S20738; S20738.
DR AlphaFoldDB; P17514; -.
DR SMR; P17514; -.
DR STRING; 4097.P17514; -.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Pathogenesis-related protein;
KW Plant defense; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT CHAIN 25..253
FT /note="Acidic endochitinase Q"
FT /id="PRO_0000005337"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT DISULFID 212..244
FT /evidence="ECO:0000250"
FT VARIANT 54
FT /note="Y -> F (in strain: cv. Samsun)"
SQ SEQUENCE 253 AA; 27633 MW; 0DED41DEA99CE196 CRC64;
MEFSGSPMAL FCCVFFLFLT GSLAQGIGSI VTSDLFNEML KNRNDGRCPA NGFYTYDAFI
AAANSFPGFG TTGDDTARRK EIAAFFGQTS HETTGGSLSA EPFTGGYCFV RQNDQSDRYY
GRGPIQLTNR NNYEKAGTAI GQELVNNPDL VATDATISFK TAIWFWMTPQ DNKPSSHDVI
IGRWTPSAAD QAANRVPGYG VITNIINGGI ECGIGRNDAV EDRIGYYRRY CGMLNVAPGE
NLDCYNQRNF GQG