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P11797 (CHIB_SERMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitinase B

EC=3.2.1.14
Gene names
Name:chiB
OrganismSerratia marcescens
Taxonomic identifier615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Contains 1 chitin-binding type-3 domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

chitinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141
Chain42 – 499458Chitinase B
PRO_0000011909

Regions

Domain438 – 49861Chitin-binding type-3

Sites

Active site1441Proton donor By similarity

Secondary structure

......................................................................................... 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11797 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: FFD674916109D1D8

FASTA49955,464
        10         20         30         40         50         60 
MSTRKAVIGY YFIPTNQINN YTETDTSVVP FPVSNITPAK AKQLTHINFS FLDINSNLEC 

        70         80         90        100        110        120 
AWDPATNDAK ARDVVNRLTA LKAHNPSLRI MFSIGGWYYS NDLGVSHANY VNAVKTPAAR 

       130        140        150        160        170        180 
TKFAQSCVRI MKDYGFDGVD IDWEYPQAAE VDGFIAALQE IRTLLNQQTI ADGRQALPYQ 

       190        200        210        220        230        240 
LTIAGAGGAF FLSRYYSKLA QIVAPLDYIN LMTYDLAGPW EKITNHQAAL FGDAAGPTFY 

       250        260        270        280        290        300 
NALREANLGW SWEELTRAFP SPFSLTVDAA VQQHLMMEGV PSAKIVMGVP FYGRAFKGVS 

       310        320        330        340        350        360 
GGNGGQYSSH STPGEDPYPN ADYWLVGCDE CVRDKDPRIA SYRQLEQMLQ GNYGYQRLWN 

       370        380        390        400        410        420 
DKTKTPYLYH AQNGLFVTYD DAESFKYKAK YIKQQQLGGV MFWHLGQDNR NGDLLAALDR 

       430        440        450        460        470        480 
YFNAADYDDS QLDMGTGLRY TGVGPGNLPI MTAPAYVPGT TYAQGALVSY QGYVWQTKWG 

       490 
YITSAPGSDS AWLKVGRLA 

« Hide

References

[1]"Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466."
Harpster M.H., Dunsmuir P.
Nucleic Acids Res. 17:5395-5395(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 990 / QMB1466.
[2]"Genetic analysis of the chitinase system of Serratia marcescens 2170."
Watanabe T., Kimura K., Sumiya T., Nikaidou N., Suzuki K., Suzuki M., Taiyoji M., Ferrer S., Regue M.
J. Bacteriol. 179:7111-7117(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 2170.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15208 Genomic DNA. Translation: CAA33278.1.
AB015997 Genomic DNA. Translation: BAA31568.1.
PIRS04856.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6NX-ray2.25A/B1-497[»]
1GOIX-ray1.45A/B1-497[»]
1H0GX-ray2.00A/B1-497[»]
1H0IX-ray2.00A/B1-497[»]
1O6IX-ray1.70A/B1-497[»]
1OGBX-ray1.85A/B1-497[»]
1OGGX-ray1.97A/B1-497[»]
3WD0X-ray1.70A2-499[»]
3WD1X-ray2.30A2-499[»]
3WD2X-ray2.20A2-499[»]
3WD3X-ray2.20A2-499[»]
3WD4X-ray2.00A2-499[»]
ProteinModelPortalP11797.
SMRP11797. Positions 3-499.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP11797.
ChEMBLCHEMBL5348.

Protein family/group databases

CAZyCBM5. Carbohydrate-Binding Module Family 5.
GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17689.
BRENDA3.2.1.14. 5690.
SABIO-RKP11797.

Family and domain databases

Gene3D2.10.10.20. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProIPR003610. CBM_fam5/12.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02839. CBM_5_12. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTSM00495. ChtBD3. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11797.

Entry information

Entry nameCHIB_SERMA
AccessionPrimary (citable) accession number: P11797
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 11, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries