ID   CHI2_SOLTU              Reviewed;         316 AA.
AC   P52404;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Endochitinase 2;
DE            EC=3.2.1.14;
DE   Flags: Precursor; Fragment;
GN   Name=CHTB2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Datura; TISSUE=Leaf;
RX   PubMed=8111037; DOI=10.1007/bf00020173;
RA   Beerhues L., Kombrink E.;
RT   "Primary structure and expression of mRNAs encoding basic chitinase and
RT   1,3-beta-glucanase in potato.";
RL   Plant Mol. Biol. 24:353-367(1994).
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: Vacuole {ECO:0000250}. Note=Vacuolar and
CC       protoplast. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Highest levels in younger leaves or stems segments
CC       and in older ones. Leaves and stems of intermediate age show a
CC       decreased expression. Appreciable amounts are also found in old root
CC       segments, and carpels.
CC   -!- INDUCTION: In response to infection, elicitor, ethylene, wounding.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily. {ECO:0000305}.
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DR   EMBL; U02606; AAA17408.1; -; mRNA.
DR   PIR; S65020; S65020.
DR   AlphaFoldDB; P52404; -.
DR   SMR; P52404; -.
DR   STRING; 4113.PGSC0003DMT400069033; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   EnsemblPlants; RHC10H1G1777.2.1; RHC10H1G1777.2.1; RHC10H1G1777.2.
DR   Gramene; RHC10H1G1777.2.1; RHC10H1G1777.2.1; RHC10H1G1777.2.
DR   eggNOG; KOG4742; Eukaryota.
DR   InParanoid; P52404; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P52404; baseline.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
DR   PROSITE; PS00774; CHITINASE_19_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Reference proteome; Signal; Vacuole.
FT   SIGNAL          <1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..309
FT                   /note="Endochitinase 2"
FT                   /id="PRO_0000005322"
FT   PROPEP          310..316
FT                   /note="Removed in mature form, vacuolar targeting"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005323"
FT   DOMAIN          19..60
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   DISULFID        21..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        30..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        54..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        87..150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        162..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        269..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   NON_TER         1
SQ   SEQUENCE   316 AA;  33629 MW;  81FB3DB3F222A0C6 CRC64;
     EFTTLFLLFS VLLLSASAEQ CGSQAGGALC ASGLCCSKFG WCGNTNDYCG PGNCQSQCPG
     GSPGDLGGVI SNSMFDQMLN HRNDNACQGK GNFYSYNAFI SAAGSFPGFG TTGDITARKR
     EIAAFFAQTS HETTGGWASA PDGPYAWGYC FLREQGSPGD YCTPSNQWPC APGRKYFGRG
     PIQISHNYNY GPCGRAIGVD LLNNPDLVAT DSIISFKSAI WFWMTPQSPK PSCHDVITGR
     WQPSGTDQAA NRVPGFGVIT NIINGGLECG HGSDSRVQDR IGFYRRYCGI LGVSPGDNLD
     CGNQRSFGNG LLVDTV