ID S5UXX2_STRC3 Unreviewed; 607 AA.
AC S5UXX2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=B446_26600 {ECO:0000313|EMBL:AGS72128.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS72128.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS72128.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(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; CP006259; AGS72128.1; -; Genomic_DNA.
DR RefSeq; WP_020942543.1; NC_021985.1.
DR AlphaFoldDB; S5UXX2; -.
DR STRING; 1214242.B446_26600; -.
DR KEGG; sci:B446_26600; -.
DR PATRIC; fig|1214242.5.peg.5450; -.
DR eggNOG; COG3469; Bacteria.
DR HOGENOM; CLU_019399_1_1_11; -.
DR Proteomes; UP000015423; 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:UP000015423};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..607
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004533085"
FT DOMAIN 182..263
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 274..607
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 607 AA; 63095 MW; 934E06274E8ED8C9 CRC64;
MDRARPARSA GRPRSVLALL TAALLAVPGV TALSSAAVAA DADLVRNGGF ESGLDNWSCT
AGKTVGSPVH GGSAALQATP AGSDNAQCAQ TVTVQPNAQY TLSGYVRGSY VYLGASGTGT
TDVSSWTQSA PDWQKLTTTF TTGAATTKVT LYTHGWYGTG AYYADDVSLV GPGGGTAQPP
APPTGLKAGT VTSSSVALSW SAVTGATGYA VYRDGVKTQT VSGTSATVSG LAAATAYSFQ
VTAANDAGES AKSAAVTATT SAGTGGGSPG LPAHALVGYL HTTFANGSGY TRLADVPDSW
DVIDLAFGEP TSVTSGDIRF NRCPVTECPN VESDADFKAA IKAKQAAGKK VLISIGGQNG
QVQLTTAAAR DTFVSSVSKI IDDYGLDGLD IDFEGHSLSL NTNDTDFRNP TTPVIVNLIS
ALKTLKAKYG AAFVLTMAPE TFFVQNGYQF YGTGKWGGQD PRCGAYLPVI HALRDDLTLL
HVQDYNSGPI MGLDNQYHSM GGADFHIAMT DMLLTGFPVA GDPNNVFPPL RPDQVAIGMP
ASTNAGNGYV SPAEVTRTLD CLTKRTNCGS YTPHGTWPAL RGLMTWSVNW DRYANWEFQK
NFDAYFG
//
