ID   CHIA_TOBAC              Reviewed;         291 AA.
AC   P29060; P82433;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Acidic endochitinase;
DE            EC=3.2.1.14;
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].
RC   STRAIN=cv. Xanthi; TISSUE=Leaf;
RX   PubMed=1643280; DOI=10.1007/bf00027070;
RA   Lawton K., Ward E., Payne G., Moyer M., Ryals J.;
RT   "Acidic and basic class III chitinase mRNA accumulation in response to TMV
RT   infection of tobacco.";
RL   Plant Mol. Biol. 19:735-743(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-36, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Petit Havana;
RX   PubMed=11289605; DOI=10.1007/s004250000407;
RA   Blee K.A., Wheatley E.R., Bonham V.A., Mitchell G.P., Robertson D.,
RA   Slabas A.R., Burrell M.M., Wojtaszek P., Bolwell G.P.;
RT   "Proteomic analysis reveals a novel set of cell wall proteins in a
RT   transformed tobacco cell culture that synthesises secondary walls as
RT   determined by biochemical and morphological parameters.";
RL   Planta 212:404-415(2001).
CC   -!- FUNCTION: This protein functions as a defense against chitin containing
CC       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, cell wall
CC       {ECO:0000269|PubMed:11289605}.
CC   -!- INDUCTION: By TMV infection.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; Z11563; CAA77656.1; -; mRNA.
DR   PIR; S23544; S23544.
DR   RefSeq; NP_001313082.1; NM_001326153.1.
DR   AlphaFoldDB; P29060; -.
DR   SMR; P29060; -.
DR   STRING; 4097.P29060; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GeneID; 107825584; -.
DR   KEGG; nta:107825584; -.
DR   OMA; IRACQNQ; -.
DR   PhylomeDB; P29060; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
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; Cell wall; Chitin degradation;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:11289605"
FT   CHAIN           23..291
FT                   /note="Acidic endochitinase"
FT                   /id="PRO_0000011918"
FT   DOMAIN          23..291
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        149
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        42..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        180..209
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  31283 MW;  B843116D10DD14D3 CRC64;
     MIKYSFLLTA LVLFLRALKL EAGDIVIYWG QNGNEGSLAD TCATNNYAIV NIAFLVVFGN
     GQNPVLNLAG HCDPNAGACT GLSNDIRACQ NQGIKVMLSL GGGAGSYFLS SADDARNVAN
     YLWNNYLGGQ SNTRPLGDAV LDGIDFDIEG GTTQHWDELA KTLSQFSQQR KVYLTAAPQC
     PFPDTWLNGA LSTGLFDYVW VQFYNNPPCQ YSGGSADNLK NYWNQWNAIQ AGKIFLGLPA
     AQGAAGSGFI PSDVLVSQVL PLINGSPKYG GVMLWSKFYD NGYSSAIKAN V