ID   B1IJ94_CLOBK            Unreviewed;       504 AA.
AC   B1IJ94;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Glycosyl hydrolase, family 18 {ECO:0000313|EMBL:ACA46835.1};
GN   OrderedLocusNames=CLD_3356 {ECO:0000313|EMBL:ACA46835.1};
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA46835.1, ECO:0000313|Proteomes:UP000008541};
RN   [1] {ECO:0000313|EMBL:ACA46835.1, ECO:0000313|Proteomes:UP000008541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; CP000939; ACA46835.1; -; Genomic_DNA.
DR   RefSeq; WP_015958164.1; NC_010516.1.
DR   AlphaFoldDB; B1IJ94; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   KEGG; cbb:CLD_3356; -.
DR   HOGENOM; CLU_037415_4_1_9; -.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02874; GH18_CFLE_spore_hydrolase; 1.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR041704; CFLE_GH18.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   PANTHER; PTHR46066:SF2; CHITINASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46066; CHITINASE DOMAIN-CONTAINING PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF08239; SH3_3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SMART; SM00257; LysM; 2.
DR   SMART; SM00287; SH3b; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS51782; LYSM; 2.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          7..50
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          53..96
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          99..161
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          170..502
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   504 AA;  57373 MW;  3113FE4D3BD48B21 CRC64;
     MWRQPNISYI VKPGDSLFTI ARSYGITVEQ LKEYNGLVSN DLYVGQQIFI PISIYKVQRG
     DSLYYIAKKF DTTVESLMVL NNLDSINLNI GQILYIPLYT EAIMKVEDGN IRSQPSINSK
     ILYKMAKGAK LPIIGVYKDF YKIKLFNGNE GFVSKAIVDF KTYGNMKPVV AVDGFYTLEE
     GETLPSSYES FVTNINLISE ICLFMFRIDP SDATAIEKFG DFTDEYVKEL VNIAHRNNVR
     VLAVVHNLLY RPGGTTKAKD LVKSLVSTRE NRQIFINNLI SLIEKYNFDG VNIDIEDVYI
     EDKDNLSSLY LEMGREFRRK GYFLSASIPS RVSDEPFNPF SDPFDYRIIG SAVDEFIVML
     YNEHGWPGSG PGPVVSIGWM NRVLNYTITR VPRNKVVAAV SVFGFDFNLT TGRNTYVTYA
     GAIEIAKRYG KDIIFDEETK TPMFSYVDEN GNNHEVWFEN AESIYAKAEL AFNKGIKGIA
     LWRLGMEDNK IWDSMKKDIV VKMA
//