ID S5UX91_STRC3 Unreviewed; 608 AA.
AC S5UX91;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Chitinase C {ECO:0000313|EMBL:AGS71853.1};
GN ORFNames=B446_25210 {ECO:0000313|EMBL:AGS71853.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS71853.1, 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:AGS71853.1, 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}.
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; CP006259; AGS71853.1; -; Genomic_DNA.
DR RefSeq; WP_020942277.1; NC_021985.1.
DR AlphaFoldDB; S5UX91; -.
DR SMR; S5UX91; -.
DR STRING; 1214242.B446_25210; -.
DR KEGG; sci:B446_25210; -.
DR PATRIC; fig|1214242.5.peg.5167; -.
DR eggNOG; COG3325; Bacteria.
DR HOGENOM; CLU_002833_14_4_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: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; 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; 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|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004533079"
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..608
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 135..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 62957 MW; 47DEA5E2F2593DC4 CRC64;
MRFRHRAAAG FATLLLPLAG LVGLASPAQA ATNATASFAK TSDWGTGFGG QWTIKNTGTS
SIGSWTVEWD FPSGTSVTSA WDADVTNSGT HWTAKNKSYN GTLAPGASVS FGFNGAGPGS
PSNCKLNGDS CDGTTVPGDA APSAPGTPTA SGITDTSVKL NWSAATDDKG VKNYDVLRDG
SKVATVTGTS YTDSGLTAGT DYSYTVQARD TADQTGPVSG AVKVHTTGGG TTPPPTGGDK
VKLGYFTEWG IYGRNYNVKN LVTSGSAAKI THINYAFGNV TNGQCAIGDS YADYDKAFTA
DQSVSGVADT WDQPLRGNFN QLRELKAKYP NLKVIWSFGG WTWSGGFAQA AANPTAFAQS
CYNLVEDPRW ADVFDGIDID WEYPNACGLS CDTSGAAAFK NVMSALRAKF GSKALVTAAV
TADGSAGGKI EAADYAGAAQ SVDWYNVMTY DFFGAWDAKG PTAPHSPLTS YSGIPKDGFT
TADAMAKYKA AGVPASKLLI GIGFYGRGWT GVTQDAPGGT ATGPAAGTYE QGIEDYKVLK
TSCPANGTVA GTAYAHCGSN WWSYDTPATI ASKMTWAKNQ GLGGAFFWEF SGDTSNGELV
SAINSGLS
//
