ID Q9L115_STRCO Unreviewed; 791 AA.
AC Q9L115;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:CAB76866.1};
GN OrderedLocusNames=SCO1444 {ECO:0000313|EMBL:CAB76866.1};
GN ORFNames=SCL6.01 {ECO:0000313|EMBL:CAB76866.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB76866.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB76866.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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DR EMBL; AL939108; CAB76866.1; -; Genomic_DNA.
DR RefSeq; NP_625725.1; NC_003888.3.
DR RefSeq; WP_011027789.1; NZ_VNID01000029.1.
DR AlphaFoldDB; Q9L115; -.
DR STRING; 100226.gene:17759030; -.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; 100226-SCO1444; -.
DR PATRIC; fig|100226.15.peg.1454; -.
DR eggNOG; COG3325; Bacteria.
DR eggNOG; COG3979; Bacteria.
DR HOGENOM; CLU_002833_13_0_11; -.
DR InParanoid; Q9L115; -.
DR OrthoDB; 3882626at2; -.
DR PhylomeDB; Q9L115; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR009470; Chi_C.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF308; CHITINASE A; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF06483; ChiC; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..791
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030176809"
FT DOMAIN 78..554
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 707..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 84456 MW; 601CDDBE1887B68C CRC64;
MPSPSRSRSR HRAGPALFAA VAAVAGLLLA GLPATASQAA DQESCRPDGL YQTPGVDVPY
CSVYDADGRE KMGADHPRRV IGYFTSWRTG KDGKPAYLAS DIPWDKITHI NYAFAHVDGG
NRLSVGSDGE KNAATGMTWP GVEGAEMDPG LPYKGHFNLL NKFKKQHPDV KTMISVGGWA
ETGGYFADDG SRVDSGGFYS MATKADGSVN QAGIDTFADS AVDFVRKYGF NGVDIDYEYP
TTMKDAGNPL DWSFANGRRA GLVKGYAALM KTLREKLDRA GAADGRHYLL SVAAPSSGYL
LRGMETFQVQ KYLDYVNIMS YDLHGAWNEY VGPNASLFDD GRDAELAAAN VYGSAQYGGI
GYLNTDWAYH YFRGSMPAGR INIGLPYYTR GHKNVQGGTD GLWGRASAST CPAGSGLTKC
GDGAVGIDNL WHDLDTNGKE SPAGSNPMWH AKNLEKGIVG DYVTDYGFPA DTKLTGTYAR
KYDSTLVAPW LWNAEKKVFL STEDEQSVGA KADYVADRGI GGAMIWELAG DYGWNAAKGQ
YEMGDTLTSL MYDTFRSAAP YGAKKSDADL PVRAVDVDVE FTDFKLGDSN YPITPKLRIT
NNTRTALPGG TEFQFDYGTS APGNASDQSG FGTKVIHSDH TGGNAGGLKG DFHRVSLKLP
AWQSLAPGAT VDLAFNYYLP VSTPSNWTVT IGGTAYALAG DLARGTTVVD PGTQTPTPTP
TPTGTESPGP SPSPTDGTGQ CTAPAWDTAS SYGGGTTVSH QGHTWKSKWW TKGEEPGTTG
EWGVWQDLGA C
//
