ID F5A7H7_BACTU Unreviewed; 676 AA.
AC F5A7H7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Endochitinase {ECO:0000313|EMBL:AEB21643.1};
OS Bacillus thuringiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428 {ECO:0000313|EMBL:AEB21643.1};
RN [1] {ECO:0000313|EMBL:AEB21643.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MR21 {ECO:0000313|EMBL:AEB21643.1};
RX PubMed=23456349; DOI=10.1007/s12223-013-0233-y;
RA Rosas-Garcia N.M., Fortuna-Gonzalez J.M., Barboza-Corona J.E.;
RT "Characterization of the chitinase gene in Bacillus thuringiensis Mexican
RT isolates.";
RL Folia Microbiol. (Praha) 58:483-490(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; HQ418217; AEB21643.1; -; Genomic_DNA.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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; PS50853; FN3; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 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}.
FT DOMAIN 41..478
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 486..578
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 574..676
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 676 AA; 74491 MW; 45BB87E2EFF408ED CRC64;
MAMRSQKFTL LLLSLLLFLP LFLTNFITPN LALADSPKQS QKIVGYFPSW GVYGRNYQVA
DIDASKLTHL NYAFADICWN GKHGNPSTHP DNPNKQTWNC KESGVPLQNK EVPNGTLVLG
EPWADVTKSY PGSGTTWEDC DKYARCGNFG ELKRLKAKYP HLKTIISVGG WTWSNRFSDM
AADEKTRKVF AESTVAFLRA YGFDGVDLDW EYPGVETIPG GSYRPEDKQN FTLLLQDVRX
ALNKAGAEDG KQYLLTIASG ASQRYADHTE LKKISQILDW INIMTYDFHG GWEATSNHNA
ALYKDPNDPA ANTNFYVDGA INVYTNEGVP VDKLVLGVPF YGRGWKSCGK ENNGQYQPCK
PGSDGKLASK GTWDDYSTGD TGVYDYGDLA ANYVNKNGFV RYWNDTAKVP YLYNATTGTF
ISYDDNESMK YKTDYIKTKG LSGAMFWELS GDCRTSPKYS CSGPKLLDTL VKELLGGPIN
QKDTEPPTNV KNIVVTNKNS NSVQLNWTAS TDNVGVTEYE ITAGEEKWST TTNSITIKNL
KPNTEYKFSI IAKDAAGNKS QPTALTVKTD EANTTPPDGN GTATFSVTSN WGSGYNFSII
IKNNGTTPIK NWKLEFDYSG NLTQVWDSKI SSKTNNHYVI TNAGWNGEIP PGGSITIGGA
GTGNPAELLN TVISEN
//
