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Database: UniProt
Entry: A0A089XAI7_STRGA
LinkDB: A0A089XAI7_STRGA
Original site: A0A089XAI7_STRGA 
ID   A0A089XAI7_STRGA        Unreviewed;       566 AA.
AC   A0A089XAI7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=SGLAU_21525 {ECO:0000313|EMBL:AIS00259.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIS00259.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT   GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT   plasmid.";
RL   J. Biotechnol. 194:81-83(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   EMBL; CP009438; AIS00259.1; -; Genomic_DNA.
DR   RefSeq; WP_043503728.1; NZ_CP009438.1.
DR   AlphaFoldDB; A0A089XAI7; -.
DR   STRING; 1907.SGLAU_21525; -.
DR   KEGG; sgu:SGLAU_21525; -.
DR   eggNOG; COG3469; Bacteria.
DR   HOGENOM; CLU_019399_1_1_11; -.
DR   OMA; WYGQAAY; -.
DR   OrthoDB; 5172397at2; -.
DR   Proteomes; UP000029482; Chromosome.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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: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:UP000029482};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..566
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001851616"
FT   DOMAIN          184..265
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          276..566
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   566 AA;  57360 MW;  348ABFB0DA34E2B0 CRC64;
     MDPVRRRSRR IRLWSGAATA ALALSLTTAT QASAADVNNV RNAGFEAGLA DWTCSAGSGT
     AVSSPVHGGT AALKATPAGQ DNARCTQTVA VRPDSTYTLS AWVQGGYAYL GATGTGTTDV
     STWTPGSTGW KQLTTTFTTG ASTTSVTVYT HGWYGQAAYH VDDVSVLGPD GGGGGGPAPT
     VPGAPAGLSV AGTTSSSVSL SWNTVSGATG YTVYRNGTKA TAVTGTSATV TGLAASTAYS
     FQVTATNAAG ESPKSATVTA TTAPAGGGGG GSLPKHAVTG YWQNFNNGAA VQRLSDVQAQ
     YDIIAVAFAD ATSTPGAVTF NLDSAGLGGY TVDQFKADIK AKQAAGKKVI ISVGGELGRV
     AVNDATSAAN FANSVHSLMQ TYGFDGVDID LENGLNATYM TQALRSLSAK AGPSLIITMA
     PQTIDMQSTS NSYFQTALNI KDILTVVNMQ YYNSGSMLGC DGKVYSQGSV DFLTALACIQ
     LENGLAPSQV GLGVPASTRG AGSGYVAPSV VNAALDCLTK ATNCGSFKPP RTYPDLRGAM
     TWSTNWDATA GNAWSNAVGP HVHALP
//
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