ID   CHIT_STRLI              Reviewed;         619 AA.
AC   P36909;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Chitinase C;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=chiC;
OS   Streptomyces lividans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8515228; DOI=10.1099/00221287-139-4-677;
RA   Fujii T., Miyashita K.;
RT   "Multiple domain structure in a chitinase gene (chiC) of Streptomyces
RT   lividans.";
RL   J. Gen. Microbiol. 139:677-686(1993).
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   -!- INDUCTION: By chitin.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; D12647; BAA02168.1; -; Genomic_DNA.
DR   AlphaFoldDB; P36909; -.
DR   BMRB; P36909; -.
DR   SMR; P36909; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
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   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_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   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..619
FT                   /note="Chitinase C"
FT                   /id="PRO_0000011911"
FT   DOMAIN          31..134
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   DOMAIN          144..229
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          240..619
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          212..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        382
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         312..313
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         339..342
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         383
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         449..452
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   BINDING         589
FT                   /ligand="chitin"
FT                   /ligand_id="ChEBI:CHEBI:17029"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   619 AA;  65200 MW;  A23CEE5B3C5D6F21 CRC64;
     MRFRHKAAAL AATLALPLAG LVGLASPAQA ATSATATFAK TSDWGTGFGG SWTVKNTGTT
     SLSSWTVEWD FPTGTKVTSA WDATVTNSGD HWTAKNVGWN GTLAPGASVS FGFNGSGPGS
     PSNCKLNGGS CDGTSVPGDA APSAPGTPTA SNITDTSVKL SWSAATDDKG VKNYDVLRDG
     AKVATVTGTT YTDNGLTKGT AYSYSVKARD TADQTGPASG AVKVTTTGGG DGGNPGTGAE
     VKMGYFTNWG VYGRNYHVKN LVTSGSADKI THINYAFGNV QGGKCTIGDS YADYDKAYTA
     DQSVDGVADT WDQPLRGNFN QLRKLKAKYP NIKILYSFGG WTWSGGFPDA VKNPAAFAKS
     CHDLVEDPRW ADVFDGIDLD WEYPNACGLS CDETSAPNAF SSMMKAMRAE FGQDYLITAA
     VTADGSDGGK IDAADYGEAS KYIDWYNVMT YDFFGAWAKN GPTAPHSPLT AYDGIPQQGF
     NTADAMAKFK SKGVPADKLL IGIGFYGRGW TGVTQSAPGG TATGPATGTY EAGIEDYKVL
     KNSCPATGTI AGTAYAHCGS NWWSYDTPAT IKSKMDWAEQ QGLGGAFFWE FSGDTANGDW
     WRHRQRPQVT PAVRTTRRH
//