CHIP_BETVU
ID CHIP_BETVU Reviewed; 288 AA.
AC P42820;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Acidic endochitinase SP2;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=SP2;
OS Beta vulgaris (Sugar beet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX NCBI_TaxID=161934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND PYROGLUTAMATE
RP FORMATION AT GLN-28.
RC STRAIN=cv. Monova; TISSUE=Leaf;
RX PubMed=8018873; DOI=10.1007/bf00023241;
RA Nielsen K.K., Bojsen K., Roepstorff P., Mikkelsen J.D.;
RT "A hydroxyproline-containing class IV chitinase of sugar beet is
RT glycosylated with xylose.";
RL Plant Mol. Biol. 25:241-257(1994).
CC -!- FUNCTION: Defense against chitin-containing fungal pathogens.
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Localized to infected area.
CC -!- INDUCTION: By infection with Cercospora beticola.
CC -!- PTM: O-glycosylated on hydroxyprolines; contains xylose.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; L25826; AAA32916.1; -; mRNA.
DR PIR; S46536; S46536.
DR AlphaFoldDB; P42820; -.
DR SMR; P42820; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00182; Glyco_hydro_19; 2.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Hydroxylation; Plant defense; Polysaccharide degradation;
KW Pyrrolidone carboxylic acid; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT CHAIN 28..288
FT /note="Acidic endochitinase SP2"
FT /id="PRO_0000005289"
FT DOMAIN 28..63
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT REPEAT 67..69
FT /note="1"
FT REPEAT 70..72
FT /note="2"
FT REPEAT 73..75
FT /note="3"
FT REPEAT 76..78
FT /note="4"
FT REGION 64..85
FT /note="Hinge region (Gly/Pro/Thr-rich)"
FT REGION 64..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..78
FT /note="4 X 3 AA tandem repeats of T-T-P"
FT REGION 86..288
FT /note="Catalytic"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT MOD_RES 28
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:8018873"
FT MOD_RES 66
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 30..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 32..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 37..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 56..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 107..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 168..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 256..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 288 AA; 30417 MW; 7F258723506BA933 CRC64;
MTLLLKNTLY LALIISVISS FPTSLFAQNC GCAPNLCCSN FGFCGTGTPY CGVGNCQSGP
CEGGTPTTPT TPTTPTTPGT GGGGSSVSDI VSQAFFDGII GQAAASCPGK NFYTRAAFLS
AVDPKFGNEG SSDDNKREIA AFFAHISHET TNLCHIEERD GDVGDAYCDQ DKAAQYPCAA
GKKYYGRGPL QLSWNYNYAL AGQAIGFDGL GNPEKVATDV NTSFKAAMWF WMTNVHSVMN
QGFGATTKAI NGALECNGQN QDQANDRIQF YKKYCADFGV APGDNLTC
