ID A0A1B8W7B3_9BACI Unreviewed; 780 AA.
AC A0A1B8W7B3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=A7975_15960 {ECO:0000313|EMBL:OBZ12512.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ12512.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ12512.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ12512.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBZ12512.1}.
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DR EMBL; MAQX01000022; OBZ12512.1; -; Genomic_DNA.
DR RefSeq; WP_065386158.1; NZ_MAQX01000022.1.
DR AlphaFoldDB; A0A1B8W7B3; -.
DR Proteomes; UP000092623; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12214; ChiA1_BD; 1.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
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 6, ISOFORM C; 1.
DR Pfam; PF02839; CBM_5_12; 2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50853; FN3; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092623};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..780
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008618246"
FT DOMAIN 40..453
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 479..564
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 639..724
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 457..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 80784 MW; C8685005764C3D5D CRC64;
MKKRMKKAST LVMLAAMLLS AVGLFVPAAS TQAAAANNSY KVIGYFPAWG AYGRGYNVTD
IDASKLTHIN YAFADICWNG SHGNPDPTGP NPATWSCQNE AGAITVPNGT IVLGDPWIDA
QKAYAGDAWD KPLKGNIGQL IKLKQANPHL RTIISIGGWS WSNRFSDVAA SSATRSVFAK
SAVDFIRHYQ FDGVDLDWEY PVNGGLAGNS ARPEDKHNYT LLLQEVRKEL DAAEIVDGKT
YELTIASGAS PSYVNNTELA QIAATVDWIN IMTYDFNGGW STKSAHNAPL YTDSAAVQAG
IPNADTFNVA KGVQGHLDAG VPANKLVLGV PFYGRGWSGC AAGPNGDGQY QTCASTPPAG
TWEAGVFDYG DLAAKYINKN GFVRYWNDVA KVPYLYNAAS KVFISYDDYE SFGYKIDYLK
TKGLAGGMFW ELSSDCRVSG NYSCSGNKLL DKLAGDLNNG GTPGGGNPTD PADTTAPSTP
ANLTSTAKTS SSVTLSWSAS TDNKGVTGYQ VYNAAALAAT VTGTSATISG LTAETAYSFT
VKAKDAAGNL SAASAAVSVT TAAAPTGTCP AAEWASATAY SGGQQVKYNG TVYEAKWWTQ
GDRPDQSGAW GVWKVIGPCG SGGGGTTTPV PVDTAAPSTP AGLTVAGQTT SSVSLSWSAS
SDNTGVTGYE VFNGSTLIAQ SATASIVVSG LSAGTTYHFT VKAKDAAGNR SAASSQVSVT
LAASGGGGNG TGAAAWSAGV SYHAGDLVSY GGVTYKCLQP HSAIVGWEPA NVLALWQAQA
//