Reviewed, UniProtKB/Swiss-Prot P33665 (CHIS_STRSN)

Names and origin

Protein names

Recommended name:
    Chitosanase
    EC=3.2.1.132

Gene names

Name:	csn
Synonyms:	chs

Organism

Streptomyces sp. (strain N174)

Taxonomic identifier

69019 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	278 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	Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.
Catalytic activity	Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 46 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chitosanase 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 – 40

40

Ref.2

Chain

41 – 278

238

Chitosanase

PRO_0000012209

Sites

Active site

62

1

Proton donor

Active site

80

1

Nucleophile

Experimental info

Mutagenesis

62

1

E → D or Q: Drastic reduction of activity.

Mutagenesis

80

1

D → E or N: Drastic reduction of activity.

Secondary structure

1

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278

Helix Strand Turn

Details...

Helix

44 – 46

3

Helix

48 – 62

15

Beta strand

63 – 66

4

Helix

68 – 71

4

Beta strand

75 – 77

3

Beta strand

79 – 82

4

Beta strand

84 – 86

3

Turn

87 – 90

4

Turn

93 – 95

3

Helix

97 – 108

12

Helix

115 – 117

3

Helix

118 – 124

7

Helix

134 – 144

11

Helix

148 – 161

14

Helix

163 – 172

10

Helix

177 – 190

14

Beta strand

192 – 195

4

Helix

199 – 209

11

Helix

213 – 215

3

Helix

219 – 236

18

Helix

244 – 247

4

Helix

250 – 255

6

Beta strand

265 – 269

5

Beta strand

272 – 276

5

Sequences

	Sequence		Length	Mass (Da)
	P33665-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: AEB36286AA9AF95F	FASTA	278	29,835
	10 20 30 40 50 60 MHSQHRTARI ALAVVLTAIP ASLATAGVGY ASTQASTAVK AGAGLDDPHK KEIAMELVSS 70 80 90 100 110 120 AENSSLDWKA QYKYIEDIGD GRGYTGGIIG FCSGTGDMLE LVQHYTDLEP GNILAKYLPA 130 140 150 160 170 180 LKKVNGSASH SGLGTPFTKD WATAAKDTVF QQAQNDERDR VYFDPAVSQA KADGLRALGQ 190 200 210 220 230 240 FAYYDAIVMH GPGNDPTSFG GIRKTAMKKA RTPAQGGDET TYLNAFLDAR KAAMLTEAAH 250 260 270 DDTSRVDTEQ RVFLKAGNLD LNPPLKWKTY GDPYVINS

References

[1]	"Primary sequence of the chitosanase from Streptomyces sp. strain N174 and comparison with other endoglycosidases." Masson J.-Y., Denis F., Brzezinski R. Gene 140:103-107(1994) [PubMed: 8125325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Purification and characterization of a chitosanase from Streptomyces N174." Boucher I., Dupuy A., Vidal P., Neugebauer W.A., Brzezinski R. Appl. Microbiol. Biotechnol. 38:188-193(1992) Cited for: PROTEIN SEQUENCE OF 41-57, CHARACTERIZATION.
[3]	"Cloning and expression in Streptomyces lividans of a chitanase-encoding gene from the actinomycete Kitasatosporia N174 isolated from soil." Fink D., Boucher I., Denis F., Brzezinski R. Biotechnol. Lett. 13:845-850(1991) Cited for: CHARACTERIZATION.
[4]	"Reaction mechanism of chitosanase from Streptomyces sp. N174." Fukamizo T., Honda Y., Goto S., Boucher I., Brzezinski R. Biochem. J. 311:377-383(1995) [PubMed: 7487871] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Site-directed mutagenesis of evolutionary conserved carboxylic amino acids in the chitosanase from Streptomyces sp. N174 reveals two residues essential for catalysis." Boucher I., Fukamizo T., Honda Y., Willick G.E., Neugebauer W.A., Brzezinski R. J. Biol. Chem. 270:31077-31082(1995) [PubMed: 8537367] [Abstract] Cited for: MUTAGENESIS.
[6]	"X-ray structure of an anti-fungal chitosanase from streptomyces N174." Marcotte E.M., Monzingo A.F., Ernst S.R., Brzezinski R., Robertus J.D. Nat. Struct. Biol. 3:155-162(1996) [PubMed: 8564542] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07779 Genomic DNA. Translation: AAA19865.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CHK	X-ray	2.40	A/B	41-278	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH46. Glycoside Hydrolase Family 46.

Family and domain databases

InterPro

IPR000400. Glyco_hydro_46.
[Graphical view]

Pfam

PF01374. Glyco_hydro_46. 1 hit.
[Graphical view]

PIRSF

PIRSF036551. Chitosanase. 1 hit.

PROSITE

PS60000. CHITOSANASE_46_80. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CHIS_STRSN

Accession

Primary (citable) accession number: P33665

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)