ID   CHI2_STROI              Reviewed;          27 AA.
AC   P29116;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   29-SEP-2021, entry version 70.
DE   RecName: Full=Chitinase 47 kDa;
DE            EC=3.2.1.14;
DE   Flags: Fragment;
OS   Streptomyces olivaceoviridis (Streptomyces corchorusii).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1921;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 11238 / DSM 41433 / NCIB 8592 / QM B814;
RX   PubMed=1592803; DOI=10.1128/jb.174.11.3450-3454.1992;
RA   Romaguera A., Menge U., Breves R., Diekmann H.;
RT   "Chitinases of Streptomyces olivaceoviridis and significance of processing
RT   for multiplicity.";
RL   J. Bacteriol. 174:3450-3454(1992).
CC   -!- FUNCTION: Able to cleave chitin oligomers from N=3 to 6.
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   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   PIR; C44908; C44908.
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   InterPro; IPR001223; Glyco_hydro18_cat.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation.
FT   CHAIN           1..>27
FT                   /note="Chitinase 47 kDa"
FT                   /id="PRO_0000077046"
FT   DOMAIN          3..>27
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   NON_TER         27
SQ   SEQUENCE   27 AA;  3173 MW;  E9549D5E273DFEE9 CRC64;
     AGSKVVGYFT EWGTYDRKYY VKNIEXS