ID   Q9RC18_9BACI            Unreviewed;       273 AA.
AC   Q9RC18;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   04-NOV-2026, entry version 54.
DE   RecName: Full=Chitosanase {ECO:0000256|PIRNR:PIRNR036551};
DE            EC=3.2.1.132 {ECO:0000256|PIRNR:PIRNR036551};
GN   Name=choK {ECO:0000313|EMBL:AAF24188.1};
OS   Bacillus sp. KFB-CO4.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=111825 {ECO:0000313|EMBL:AAF24188.1};
RN   [1] {ECO:0000313|EMBL:AAF24188.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KFB-CO4 {ECO:0000313|EMBL:AAF24188.1};
RX   PubMed=10966383; DOI=10.1128/AEM.66.9.3727-3734.2000;
RA   Yoon H.G., Kim H.Y., Lim Y.H., Kim H.K., Shin D.H., Hong B.S., Cho H.Y.;
RT   "Thermostable chitosanase from Bacillus sp. Strain CK4: cloning and
RT   expression of the gene and characterization of the enzyme.";
RL   Appl. Environ. Microbiol. 66:3727-3734(2000).
CC   -!- FUNCTION: Aids in the defense against invading fungal pathogens by
CC       degrading their cell wall chitosan. {ECO:0000256|PIRNR:PIRNR036551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine
CC         residues in a partly acetylated chitosan.; EC=3.2.1.132;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036551, ECO:0000256|PROSITE-
CC         ProRule:PRU10070};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR036551}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 46 family.
CC       {ECO:0000256|PIRNR:PIRNR036551}.
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DR   EMBL; AF160195; AAF24188.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RC18; -.
DR   CAZy; GH46; Glycoside Hydrolase Family 46.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016977; F:chitosanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.141.10; Chitosanase, subunit A, domain 1; 1.
DR   Gene3D; 3.30.386.10; Chitosanase, subunit A, domain 2; 1.
DR   InterPro; IPR000400; Glyco_hydro_46.
DR   InterPro; IPR023099; Glyco_hydro_46_N.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF01374; Glyco_hydro_46; 1.
DR   PIRSF; PIRSF036551; Chitosanase; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS60000; CHITOSANASE_46_80; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR036551};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR036551};
KW   Secreted {ECO:0000256|PIRNR:PIRNR036551}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..273
FT                   /note="Chitosanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5054709055"
FT   ACT_SITE        43
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10070"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036551-1"
FT   ACT_SITE        66
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036551-1"
SQ   SEQUENCE   273 AA;  30552 MW;  C93916E8C9DD27B9 CRC64;
     MREADWWGKA AISLLVFTMF FTLMMSETVF AAGLNKDQKR RAEQLRRICE DGTTEMRYPY
     VARLDDARPS TCGPAGVTTA TRDGFEVVPV YKQAVANKKL PNYLAGLRRL EKEASDDTSK
     LKGPASAWKS LADDKAFRAA QDGVNDQVYY QPAMERSDNA GLTTALARAV MYHTVRQRGD
     GDDGDSRYAL IKRTPKGAGG SPKEGIDEQK CLNKFSHVRY DDLMNGANHD RRDEWRESVG
     RVHVLRSIAN QNNYNLNGGI HVRSHEYGNG VIK
//