ID CHIT_STRPL Reviewed; 610 AA.
AC P11220;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Chitinase 63;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=chtA;
OS Streptomyces plicatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces rochei group.
OX NCBI_TaxID=1922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1532161; DOI=10.1016/0378-1119(92)90604-n;
RA Robbins P.W., Overbye K., Albright C., Benfield B., Pero J.;
RT "Cloning and high-level expression of chitinase-encoding gene of
RT Streptomyces plicatus.";
RL Gene 111:69-76(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, AND PROTEIN SEQUENCE OF 31-45.
RX PubMed=3275646; DOI=10.1016/s0021-9258(19)57412-9;
RA Robbins P.W., Albright C., Benfield B.;
RT "Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63)
RT in Escherichia coli.";
RL J. Biol. Chem. 263:443-447(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- INDUCTION: By chitin.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; M82804; AAA26720.1; -; Genomic_DNA.
DR EMBL; M18397; AAA26717.1; -; Genomic_DNA.
DR PIR; JH0573; JH0573.
DR AlphaFoldDB; P11220; -.
DR SMR; P11220; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:3275646"
FT CHAIN 31..610
FT /note="Chitinase 63"
FT /id="PRO_0000011912"
FT DOMAIN 31..134
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT DOMAIN 144..229
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 241..610
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 125..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 313..314
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 340..343
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 384
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 450..453
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 590
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CONFLICT 3
FT /note="F -> I (in Ref. 2; AAA26717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 63974 MW; 6A202EF361CCD500 CRC64;
MRFRHKAAAL AATLALPLAG LVGLASPAQA ATSATATFQK TSDWGTGFGG KWTVKNTGTT
SLSSWTVEWD FPSGTKVTSA WDATVTNSAD HWTAKNVGWN GTLAPGASVS FGFNGSGPGS
PSGCKINGGS CDGSSVPGDE APSAPGTPTA SNITDTSVKL SWSAATDDKG VKNYDVLRDG
ATVATVTGTT YTDNGLTKGT DYSYSVKARD TGDQTGPASG SVKVTTTGGD GGEPNPNPGA
EVKMGYFTNW GVYGRNYHVK NLVTSGSAEK ITHINLRFGN VQGGKCTIGD AYADYDKAYT
ADQSVDGVAD TWDQPLRANF NQLRNLKAEY PHIKILYSFG GWTWSGGFPD AVKNPAAFAK
SCHDLVEDPR WADVFDGIDL DWEYPNACGL SCDETSAPNA FSSMMKAMRA EFGQDYLITA
AVTADGSDGG KIDAADYGEA SKYIDWYNVM TYDFFGAWAK NGPTAPHSPL NAYDGIPQQG
FTTADAMAKF KSKGVPADKL LIGIGFYGRG WTGVTQSAPG GTATGPAAGT YEAGIEDYKV
LKNSCPATGT VAGTAYAHCG TNWWSYDTPA TIKSKMDWAE QQGLGGAFFW EFSGDTTNGE
LVSAIDSGLK
//
