ID   CHIX_STROI              Reviewed;         597 AA.
AC   Q05638;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Exochitinase 1;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=chi01;
OS   Streptomyces olivaceoviridis (Streptomyces corchorusii).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11238 / DSM 41433 / NCIB 8592 / QM B814;
RX   PubMed=8319677; DOI=10.1111/j.1432-1033.1993.tb17966.x;
RA   Blaak H., Schnellmann J., Walter S., Henrissat B., Schrempf H.;
RT   "Characteristics of an exochitinase from Streptomyces olivaceoviridis, its
RT   corresponding gene, putative protein domains and relationship to other
RT   chitinases.";
RL   Eur. J. Biochem. 214:659-669(1993).
CC   -!- FUNCTION: Exochitinase that generates exclusively chitobiose from
CC       chitotetraose, chitohexaose, and colloidal high-molecular mass chitin.
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   -!- ACTIVITY REGULATION: Inhibited by the pseudosugar allosamidin A.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.3.;
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.;
CC   -!- INDUCTION: By chitin.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; X71080; CAA50398.1; -; Genomic_DNA.
DR   PIR; S33848; S32039.
DR   AlphaFoldDB; Q05638; -.
DR   SMR; Q05638; -.
DR   CAZy; CBM16; Carbohydrate-Binding Module Family 16.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..29
FT                   /note="Or 32"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..597
FT                   /note="Exochitinase 1"
FT                   /id="PRO_0000011910"
FT   DOMAIN          172..253
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          264..597
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        384
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   597 AA;  62314 MW;  7F5D615DD5EBC1F4 CRC64;
     MDRFRPLAVL IAAALTLSGT TALSSAARAA DADLARNGGF EAGLDGWTCT AGTTVNSPVR
     SGSSALKATP AGSDNARCAQ TVTVQPNSQY TLSGHVQGSY VYLGASGTGT TDVSTWTQSA
     PDWRQLTTTF RTGPSTTRVT LYTHGWYGTG AYHADDISLV GPGGGTEQPP APPTGLRTGS
     VTATSVALSW SPVTGATGYA VYRDGVKVAT ASGTSATVTG LTPDTAYAFQ VAAVNGAGES
     AKSATVTATT APGTGGGSAD LPPHALVGYL HASFANGSGY TRLADVPDSW DVIDLAFGEP
     TSVTSGDIRF DRCPATECPN VESDAEFKAA IKAKQAAGKK VLISIGGQNG QVQLTTTAAR
     DTFVSSVSKI IDEYGLDGLD IDFEGHSLSL NADDTDFKNP KTPVIVNLIQ ALKTLKAKYG
     DDFVLTMAPE TFFVQLGYQY YGTGKWGGQD PRAGAYLPVI HALRDDLTLL HVQDYNSGPI
     MGLDNQYHSM GGADFHIAMT DMLLTGFPVA GDAANVFPPL RADQVAIGMP ATTNAGNGHV
     APAEAVKTLD CLTRKTNCGS YATHGTWPAL RALMTWSINW DRFGGWEFQR TFDGYFG