ID   CHIT_STRVL              Reviewed;          15 AA.
AC   P84754;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Chitinase;
DE            EC=3.2.1.14;
DE   Flags: Fragment;
OS   Streptomyces violaceus (Streptomyces venezuelae).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1936;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=P10 {ECO:0000269|Ref.1};
RA   Mukherjee G.;
RT   "Extracellular production of chitinase by Streptomyces venezuelae.";
RL   Thesis (2005), Visva Bharati (Central University), India.
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=P10;
RX   PubMed=16972135; DOI=10.1007/s00284-005-0412-4;
RA   Mukherjee G., Sen S.K.;
RT   "Purification, characterization, and antifungal activity of chitinase from
RT   Streptomyces venezuelae P(10).";
RL   Curr. Microbiol. 53:265-269(2006).
CC   -!- FUNCTION: Antifungal activity. Inhibits the mycelial growth of A.niger,
CC       A.alternata and H.sativum. {ECO:0000269|PubMed:16972135,
CC       ECO:0000269|Ref.1}.
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         Evidence={ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1};
CC   -!- ACTIVITY REGULATION: Inhibited by divalent metal ions. Maximum
CC       inhibition observed with Ca(2+) while the least inhibition was observed
CC       with Fe(2+). Inhibited by high concentrations of GlcNAc.
CC       {ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6-8. There is a 37.7% decrease in activity at pH 5 and
CC         a 39.8% decrease in activity at pH 9. {ECO:0000269|PubMed:16972135,
CC         ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antimicrobial; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Direct protein sequencing; Fungicide; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..>15
FT                   /note="Chitinase"
FT                   /id="PRO_0000077047"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|PubMed:16972135, ECO:0000303|Ref.1"
SQ   SEQUENCE   15 AA;  1639 MW;  D2A2AA1786232443 CRC64;
     EQPGGDKVNL GYFTN