ID D7BRY8_STRBB Unreviewed; 549 AA.
AC D7BRY8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN OrderedLocusNames=SBI_04204 {ECO:0000313|EMBL:ADI07325.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI07325.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI07325.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI07325.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002047; ADI07325.1; -; Genomic_DNA.
DR AlphaFoldDB; D7BRY8; -.
DR STRING; 749414.SBI_04204; -.
DR CAZy; CBM16; Carbohydrate-Binding Module Family 16.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR KEGG; sbh:SBI_04204; -.
DR PATRIC; fig|749414.3.peg.4350; -.
DR eggNOG; COG3469; Bacteria.
DR HOGENOM; CLU_019399_1_1_11; -.
DR Proteomes; UP000000377; Chromosome.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_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; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..549
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003093474"
FT DOMAIN 167..248
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 259..549
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 55405 MW; DD3F122CC8606031 CRC64;
MLAAGALVAL GGGTAGAADA NLVQNSGFES GLSGWTCSSA SGTTVTSPTH GGASALKATP
AGLDNAQCTQ TVSVKPDSSY TLSAWVQGSY VYLGASGTGT TDVSTWTPSA SGWQQLTTTF
KTGPSTTSVT VYTHGWYGQP AYYADDINLT GPGGSDPGDP GDPVPTAPTG LKTGVVTSSS
IALSWSTVSG ATGYNVYRDG TKVQAVSGTS ATVTGLAAAT SYQFQVTAVN AAGESPKSAA
VTGTTSTGSG GGGGTVPKHA VTGYWQNFNN GATVQKISDV QSQYDIIAVA FADATGTPGA
VTFNLDSAGL GGYTVDQFKA DIKAKQAAGK SVIISIGGQN GTVSINDSAS ANNFANSVYS
LMQQYGFDGV DIDLENGLNA TYMTQALRSL SAKAGSKLVI TMAPQTIDMQ STSNAYFQTA
LNIKDILTVV NMQYYNSGSM LGCDGKVYSQ GSVDFLTALA CIQLEGGLSP SQVGLGLPAS
TRGAGSGYVS PTIVNNALDC LARGTGCGSF KPAKTYPGLR GAMTWSTNWD ALAGNAWSNA
VGPKVHGLP
//