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Database: UniProt
Entry: B1VYQ5_STRGG
LinkDB: B1VYQ5_STRGG
Original site: B1VYQ5_STRGG 
ID   B1VYQ5_STRGG            Unreviewed;       607 AA.
AC   B1VYQ5;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   OrderedLocusNames=SGR_1831 {ECO:0000313|EMBL:BAG18660.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG18660.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG18660.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   EMBL; AP009493; BAG18660.1; -; Genomic_DNA.
DR   RefSeq; WP_012378807.1; NC_010572.1.
DR   AlphaFoldDB; B1VYQ5; -.
DR   SMR; B1VYQ5; -.
DR   CAZy; CBM16; Carbohydrate-Binding Module Family 16.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GeneID; 6214318; -.
DR   KEGG; sgr:SGR_1831; -.
DR   PATRIC; fig|455632.4.peg.1864; -.
DR   eggNOG; COG3469; Bacteria.
DR   HOGENOM; CLU_019399_1_1_11; -.
DR   Proteomes; UP000001685; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..607
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002770114"
FT   DOMAIN          181..262
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          273..607
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   607 AA;  62969 MW;  D696CE5631261A74 CRC64;
     MERTGPTVRF SRLLAVCSAG LLAAGALAVS APTAGAADVD LARNGGFEAG LDGWTCANSS
     GAAVSTPTRS GTSALRATPA GSDHAKCSQS ITVKPNSSYT LSAWVQGSYV YLGASGTGTT
     DVSTWTQSPG AWKQLTTTFK TGPSTTSVSV YTHGWYGTPA YYADDLTLVG PGGDPVVIPA
     VPAGLKTTAI TSSSVALSWN AVSGASAYHV YRGGTKVATA TGPSATVTGL TASTAYSFQV
     TAANAAGESA KSAALTATTT AGGGGGDTKL PPRALVGYLH SSFANGSGYT RMADVPDSWD
     VINLAFGEPT SVTSGDIRFA LCPVAECPNV ESEADFKAAI KAKQAAGKKV LISIGGQNGQ
     VQLNSTAARD AFVTSVSKII DTYGLNGLDI DFEGHSLSLN TGDTDFRNPT SPVIVNLISA
     VKSLKAKYGP DFVLTMAPET FFVQLGYQFY GSGPWGGQDP RAGAYLPVIH ALRDDLTLLH
     VQDYNSGPIM GLDNQYHTMG GADFHIAMTD MLLAGFPVAG DTTKVFPGLR PDQVAIGLPA
     STQAGNGHTT PAEVNKALNC LTKKTDCGSY QTRGTWSDLR GLMTWSINWD RFNNWEFSKN
     FDAYFGS
//
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