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Reviewed, UniProtKB/Swiss-Prot P33673 (CHIS_BACCI)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Chitosanase
    EC=3.2.1.132
Gene names
Name: csn
OrganismBacillus circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionchitosanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242
Chain43 – 301259Chitosanase
PRO_0000012206

Sites

Active site791Proton donor By similarity
Active site971Nucleophile By similarity

Amino acid modifications

Disulfide bond92 ↔ 166

Secondary structure

1 ............................................ 301
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P33673-1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 5B67FB8FF1D1F763

FASTA30133,426
        10         20         30         40         50         60 
MHMSNARPSK SRTKFLLAFL CFTLMASLFG ATALFGPSKA AAASPDDNFS PETLQFLRNN 

        70         80         90        100        110        120 
TGLDGEQWNN IMKLINKPEQ DDLNWIKYYG YCEDIEDERG YTIGLFGATT GGSRDTHPDG 

       130        140        150        160        170        180 
PDLFKAYDAA KGASNPSADG ALKRLGINGK MKGSILEIKD SEKVFCGKIK KLQNDAAWRK 

       190        200        210        220        230        240 
AMWETFYNVY IRYSVEQARQ RGFTSAVTIG SFVDTALNQG ATGGSDTLQG LLARSGSSSN 

       250        260        270        280        290        300 
EKTFMKNFHA KRTLVVDTNK YNKPPNGKNR VKQWDTLVDM GKMNLKNVDS EIAQVTDWEM 


K

« Hide

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References

[1]"Primary structure of chitosanase produced by Bacillus circulans MH-K1."
Ando A., Noguchi K., Yanagi M., Shinoyama H., Kagawa Y., Hirata H., Yabuki M., Fujii T.
J. Gen. Appl. Microbiol. 38:135-144(1992)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: MH-K1.
[2]Ando A.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 119-124; 140 AND 200-202.
[3]"Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism."
Saito J., Kita A., Higuchi Y., Nagata Y., Ando A., Miki K.
J. Biol. Chem. 274:30818-30825(1999) [PubMed: 10521473] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 43-301.
Strain: MH-K1.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D10624 Genomic DNA. Translation: BAA01474.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QGIX-ray1.60A43-301[»]
2D05X-ray2.00A43-301[»]
ModBaseSearch...

Protein family/group databases

CAZyGH46. Glycoside Hydrolase Family 46.

Enzyme and pathway databases

BRENDA3.2.1.132. 1207.

Family and domain databases

InterProIPR000400. Glyco_hydro_46.
[Graphical view]
PfamPF01374. Glyco_hydro_46. 1 hit.
[Graphical view]
PIRSFPIRSF036551. Chitosanase. 1 hit.
PROSITEPS60000. CHITOSANASE_46_80. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01296. Glucosamine.

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Entry information

Entry nameCHIS_BACCI
AccessionPrimary (citable) accession number: P33673
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 1, 2004
Last modified: June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents