P42820 (CHIP_BETVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acidic endochitinase SP2
EC=3.2.1.14

Gene names

Name:

SP2

Organism

Beta vulgaris (Sugar beet)

Taxonomic identifier

161934 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Beta

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Defense against chitin containing fungal pathogens.
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Localized to infected area.
Induction	By infection with Cercospora beticola.
Post-translational modification	O-glycosylated on hydroxyprolines; contains xylose.
Sequence similarities	Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. Contains 1 chitin-binding type-1 domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Hydroxylation Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27
	Chain	28 – 288	261	Acidic endochitinase SP2		PRO_0000005289
Regions
	Domain	28 – 63	36	Chitin-binding type-1
	Repeat	67 – 69	3	1
	Repeat	70 – 72	3	2
	Repeat	73 – 75	3	3
	Repeat	76 – 78	3	4
	Region	64 – 85	22	Hinge region (Gly/Pro/Thr-rich)
	Region	67 – 78	12	4 X 3 AA tandem repeats of T-T-P
	Region	86 – 288	203	Catalytic
Amino acid modifications
	Modified residue	28	1	Pyrrolidone carboxylic acid
	Modified residue	66	1	4-hydroxyproline By similarity
	Modified residue	69	1	4-hydroxyproline By similarity
	Modified residue	72	1	4-hydroxyproline By similarity
	Modified residue	75	1	4-hydroxyproline By similarity
	Disulfide bond	30 ↔ 38		By similarity
	Disulfide bond	32 ↔ 44		By similarity
	Disulfide bond	37 ↔ 51		By similarity
	Disulfide bond	56 ↔ 61		By similarity
	Disulfide bond	107 ↔ 154		By similarity
	Disulfide bond	168 ↔ 178		By similarity
	Disulfide bond	256 ↔ 288		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42820 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 7F258723506BA933	FASTA	288	30,417
	10 20 30 40 50 60 MTLLLKNTLY LALIISVISS FPTSLFAQNC GCAPNLCCSN FGFCGTGTPY CGVGNCQSGP 70 80 90 100 110 120 CEGGTPTTPT TPTTPTTPGT GGGGSSVSDI VSQAFFDGII GQAAASCPGK NFYTRAAFLS 130 140 150 160 170 180 AVDPKFGNEG SSDDNKREIA AFFAHISHET TNLCHIEERD GDVGDAYCDQ DKAAQYPCAA 190 200 210 220 230 240 GKKYYGRGPL QLSWNYNYAL AGQAIGFDGL GNPEKVATDV NTSFKAAMWF WMTNVHSVMN 250 260 270 280 QGFGATTKAI NGALECNGQN QDQANDRIQF YKKYCADFGV APGDNLTC

References

[1]	"A hydroxyproline-containing class IV chitinase of sugar beet is glycosylated with xylose." Nielsen K.K., Bojsen K., Roepstorff P., Mikkelsen J.D. Plant Mol. Biol. 25:241-257(1994) [PubMed: 8018873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: cv. Monova. Tissue: Leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L25826 mRNA. Translation: AAA32916.1.
PIR	S46536.
3D structure databases
ProteinModelPortal	P42820.
SMR	P42820. Positions 32-59.
ModBase	Search...
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001002. Chitin-bd_1. IPR018371. Chitin-binding_1_CS. IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. IPR023346. Lysozyme-like_dom. [Graphical view]
Gene3D	G3DSA:3.30.60.10. Chitin_bd_1. 1 hit.
Pfam	PF00187. Chitin_bind_1. 1 hit. PF00182. Glyco_hydro_19. 1 hit. [Graphical view]
PIRSF	PIRSF001060. Endochitinase. 1 hit.
ProDom	PD000609. Chitin_bd_1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00270. ChtBD1. 1 hit. [Graphical view]
SUPFAM	SSF57016. Chitin_bd_1. 1 hit. SSF53955. SSF53955. 1 hit.
PROSITE	PS00026. CHIT_BIND_I_1. 1 hit. PS50941. CHIT_BIND_I_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHIP_BETVU

Accession

Primary (citable) accession number: P42820

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 31, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program