ID D6ET94_STRLI Unreviewed; 609 AA.
AC D6ET94;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Chitinase C {ECO:0000313|EMBL:EFD66692.2};
GN ORFNames=SSPG_02332 {ECO:0000313|EMBL:EFD66692.2};
OS Streptomyces lividans TK24.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457428 {ECO:0000313|EMBL:EFD66692.2};
RN [1] {ECO:0000313|EMBL:EFD66692.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TK24 {ECO:0000313|EMBL:EFD66692.2};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces lividans strain TK24.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; GG657756; EFD66692.2; -; Genomic_DNA.
DR RefSeq; WP_003973621.1; NZ_GG657756.1.
DR AlphaFoldDB; D6ET94; -.
DR HOGENOM; CLU_002833_14_4_11; -.
DR Proteomes; UP000002769; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
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 11; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 27..134
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 144..229
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 240..609
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 609 AA; 63591 MW; 5F6F69F1A4243470 CRC64;
MRFRHKAAAL AATLALPLAG LVGLASPAQA ATSATATFAK TSDWGTGFGG SWTVKNTGTT
SLSSWTVEWD FPTGTKVTSA WDATVTNSGD HWTAKNVGWN GTLAPGASVS FGFNGSGPGS
PSNCKLNGGS CDGTSVPGDA APSAPGTPTA SNITDTSVKL SWSAATDDKG VKNYDVLRDG
AKVATVTGTT YTDNGLTKGT AYSYSVKARD TADQTGPASG AVKVTTTGGG DGGNPGTGAE
VKMGYFTNWG VYGRNYHVKN LVTSGSADKI THINYAFGNV QGGKCTIGDS YADYDKAYTA
DQSVDGVADT WDQPLRGNFN QLRKLKAKYP NIKILYSFGG WTWSGGFPDA VKNPAAFAKS
CHDLVEDPRW ADVFDGIDLD WEYPNACGLS CDETSAPNAF SSMMKAMRAE FGQDYLITAA
VTADGSDGGK IDAADYGEAS KYIDWYNVMT YDFFGAWAKN GPTAPHSPLT AYDGIPQQGF
NTADAMAKFK SKGVPADKLL IGIGFYGRGW TGVTQSAPGG TATGPATGTY EAGIEDYKVL
KNSCPATGTI AGTAYAHCGS NWWSYDTPAT IKSKMDWAEQ QGLGGAFFWE FSGDTANGEL
VSAIDSGLK
//