ID   CHLY_PARTH              Reviewed;          47 AA.
AC   P23473;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Bifunctional chitinase/lysozyme;
DE   Includes:
DE     RecName: Full=Chitinase;
DE              EC=3.2.1.14;
DE   Includes:
DE     RecName: Full=Lysozyme;
DE              EC=3.2.1.17;
DE   Flags: Fragment;
OS   Parthenocissus quinquefolia (Virginia creeper) (Hedera quinquefolia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Parthenocisseae; Parthenocissus.
OX   NCBI_TaxID=3607;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Bernasconi P., Locher R., Pilet P.E., Jolles J., Jolles P.;
RT   "Purification and N-terminal amino-acid sequence of a basic lysozyme from
RT   Parthenocissus quinquifolia cultured in vitro.";
RL   Biochim. Biophys. Acta 915:254-260(1987).
CC   -!- FUNCTION: Bifunctional enzyme with lysozyme/chitinase activity.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P23473; -.
DR   SMR; P23473; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003796; F:lysozyme 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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR45708:SF21; ACIDIC ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Multifunctional enzyme; Polysaccharide degradation;
KW   Secreted.
FT   CHAIN           1..>47
FT                   /note="Bifunctional chitinase/lysozyme"
FT                   /id="PRO_0000077052"
FT   DOMAIN          1..>47
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   NON_TER         47
SQ   SEQUENCE   47 AA;  5040 MW;  1D9DCF2E7E3A0F51 CRC64;
     GGIAIYWGQN GNEGTLTQTC NTGKYSYVNI AFLNKFGNGQ TPEINLA
//