ID   CHIE_BETVU              Reviewed;         293 AA.
AC   P36910;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Acidic endochitinase SE2;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=SE2;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Monova; TISSUE=Leaf;
RX   PubMed=8400378; DOI=10.1094/mpmi-6-495;
RA   Nielsen K.K., Mikkelsen J.D., Kragh K.M., Bojsen K.;
RT   "An acidic class III chitinase in sugar beet: induction by Cercospora
RT   beticola, characterization, and expression in transgenic tobacco plants.";
RL   Mol. Plant Microbe Interact. 6:495-506(1993).
CC   -!- FUNCTION: This protein functions as a defense against chitin containing
CC       fungal pathogens. This endochitinase also exhibits exochitinase
CC       activity, i.e. it is capable of hydrolyzing chito-oligosaccharides,
CC       including chitobiose.
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, extracellular space. Note=Intercellular
CC       fluid of leaves.
CC   -!- TISSUE SPECIFICITY: Accumulates in leaves during infection.
CC   -!- INDUCTION: By fungal infection.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; S66038; AAB28479.1; -; mRNA.
DR   AlphaFoldDB; P36910; -.
DR   SMR; P36910; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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   CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR   InterPro; IPR045321; Cts1-like.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..293
FT                   /note="Acidic endochitinase SE2"
FT                   /id="PRO_0000011914"
FT   DOMAIN          26..293
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        151
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        45..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        183..212
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  30729 MW;  0E9019D28FD34123 CRC64;
     MAAKIVSVLF LISLLIFASF ESSHGSQIVI YWGQNGDEGS LADTCNSGNY GTVILAFVAT
     FGNGQTPALN LAGHCDPATN CNSLSSDIKT CQQAGIKVLL SIGGGAGGYS LSSTDDANTF
     ADYLWNTYLG GQSSTRPLGD AVLDGIDFDI ESGDGRFWDD LARALAGHNN GQKTVYLSAA
     PQCPLPDASL STAIATGLFD YVWVQFYNNP PCQYDTSADN LLSSWNQWTT VQANQIFLGL
     PASTDAAGSG FIPADALTSQ VLPTIKGSAK YGGVMLWSKA YDSGYSSAIK SSV