ID O50152_STRGR Unreviewed; 294 AA. AC O50152; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 118. DE SubName: Full=Chitinase C {ECO:0000313|EMBL:BAA23739.1}; DE EC=3.2.1.14 {ECO:0000313|EMBL:SQA23044.1}; GN Name=chiC {ECO:0000313|EMBL:BAA23739.1}; GN ORFNames=NCTC13033_02762 {ECO:0000313|EMBL:SQA23044.1}; OS Streptomyces griseus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1911 {ECO:0000313|EMBL:BAA23739.1}; RN [1] {ECO:0000313|EMBL:BAA23739.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HUT 6037 {ECO:0000313|EMBL:BAA23739.1}; RX PubMed=8752320; RA Ohno T., Sylvie A., Hata T., Nikaidou N., Bernard H., Mitsutomi M., RA Watanabe T.; RT "A modular family 19 chitinase found in the prokaryotic organism RT Streptomyces griseus HUT 6037."; RL J. Bacteriol. 178:5065-5070(1996). RN [2] {ECO:0000313|EMBL:BAA23739.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HUT 6037 {ECO:0000313|EMBL:BAA23739.1}; RA Reipen I.G., Sahm H., Sprenger G.A.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PDB:2D49} RP STRUCTURE BY NMR OF 30-81, AND DISULFIDE BONDS. RX PubMed=16567413; DOI=10.1093/jb/mvj062; RA Akagi K., Watanabe J., Hara M., Kezuka Y., Chikaishi E., Yamaguchi T., RA Akutsu H., Nonaka T., Watanabe T., Ikegami T.; RT "Identification of the substrate interaction region of the chitin-binding RT domain of Streptomyces griseus chitinase C."; RL J. Biochem. 139:483-493(2006). RN [4] {ECO:0007829|PDB:1WVU, ECO:0007829|PDB:1WVV} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 30-294, DISULFIDE BONDS, AND RP ACTIVE SITE. RX PubMed=16516924; DOI=10.1016/j.jmb.2006.02.013; RA Kezuka Y., Ohishi M., Itoh Y., Watanabe J., Mitsutomi M., Watanabe T., RA Nonaka T.; RT "Structural studies of a two-domain chitinase from Streptomyces griseus RT HUT6037."; RL J. Mol. Biol. 358:472-484(2006). RN [5] {ECO:0000313|EMBL:SQA23044.1, ECO:0000313|Proteomes:UP000251334} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC13033 {ECO:0000313|EMBL:SQA23044.1, RC ECO:0000313|Proteomes:UP000251334}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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; AB009289; BAA23739.1; -; Genomic_DNA. DR EMBL; UAVD01000026; SQA23044.1; -; Genomic_DNA. DR RefSeq; WP_003967541.1; NZ_UAVD01000026.1. DR PDB; 1WVU; X-ray; 2.45 A; A/B=30-294. DR PDB; 1WVV; X-ray; 2.00 A; A/B=30-294. DR PDB; 2D49; NMR; -; A=30-82. DR PDB; 2DBT; X-ray; 3.14 A; A/B/C=30-294. DR PDBsum; 1WVU; -. DR PDBsum; 1WVV; -. DR PDBsum; 2D49; -. DR PDBsum; 2DBT; -. DR AlphaFoldDB; O50152; -. DR SMR; O50152; -. DR STRING; 1911.GCA_001715295_03106; -. DR CAZy; CBM5; Carbohydrate-Binding Module Family 5. DR CAZy; GH19; Glycoside Hydrolase Family 19. DR GeneID; 6212097; -. DR OMA; TISTWYW; -. DR OrthoDB; 3614862at2; -. DR EvolutionaryTrace; O50152; -. DR Proteomes; UP000251334; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro. DR CDD; cd00325; chitinase_GH19; 1. DR CDD; cd00036; ChtBD3; 1. DR Gene3D; 1.10.530.10; -; 1. DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1. DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1. DR InterPro; IPR003610; CBM_fam5/12. DR InterPro; IPR036573; CBM_sf_5/12. DR InterPro; IPR016283; Glyco_hydro_19. DR InterPro; IPR000726; Glyco_hydro_19_cat. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR PANTHER; PTHR22595:SF208; CHITINASE; 1. DR PANTHER; PTHR22595; CHITINASE-RELATED; 1. DR Pfam; PF02839; CBM_5_12; 1. DR Pfam; PF00182; Glyco_hydro_19; 1. DR PIRSF; PIRSF001060; Endochitinase; 1. DR SMART; SM00495; ChtBD3; 1. DR SUPFAM; SSF51055; Carbohydrate binding domain; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1WVU, ECO:0007829|PDB:1WVV}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001060-2}; KW Glycosidase {ECO:0000313|EMBL:SQA23044.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SQA23044.1}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..29 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 30..294 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5035711770" FT DOMAIN 33..75 FT /note="Chitin-binding type-3" FT /evidence="ECO:0000259|SMART:SM00495" FT ACT_SITE 147 FT /note="EMO_00043 promote heterolysis,EMO_00066 proton FT acceptor,EMO_00068 proton donor" FT /evidence="ECO:0007829|PDB:2DBT" FT ACT_SITE 147 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001060-1" FT ACT_SITE 156 FT /note="EMO_00033 electrostatic stabiliser,EMO_00038 FT activator,EMO_00040 increase nucleophilicity,EMO_00068 FT proton donor,EMO_00066 proton acceptor" FT /evidence="ECO:0007829|PDB:2DBT" FT SITE 194 FT /note="EMO_00029 steric role,EMO_00029 steric role" FT /evidence="ECO:0007829|PDB:2DBT" FT DISULFID 32..78 FT /evidence="ECO:0007829|PDB:1WVU, ECO:0007829|PDB:1WVV" FT DISULFID 166..174 FT /evidence="ECO:0000256|PIRSR:PIRSR001060-2, FT ECO:0007829|PDB:1WVU" FT DISULFID 262..294 FT /evidence="ECO:0000256|PIRSR:PIRSR001060-2, FT ECO:0007829|PDB:1WVU" SQ SEQUENCE 294 AA; 31473 MW; 21B674EC35662634 CRC64; MYRRVMSLLV ALGAIVAALI VLPATTAQAA TCATAWSSSS VYTNGGTVSY NGRNYTAKWW TQNERPGTSD VWADKGACGT GGEGPGGNNG FVVSEAQFNQ MFPNRNAFYT YKGLTDALSA YPAFAKTGSD EVKKREAAAF LANVSHETGG LFYIKEVNEA NYPHYCDTTQ SYGCPAGQAA YYGRGPIQLS WNFNYKAAGD ALGINLLANP YLVEQDPAVA WKTGLWYWNS QNGPGTMTPH NAIVNNAGFG ETIRSINGAL ECNGGNPAQV QSRINKFTQF TQILGTTTGP NLSC //