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P0C2S1 (CELK_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 32. 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:
Cellulose 1,4-beta-cellobiosidase

EC=3.2.1.91
Gene names
Name:celK
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length895 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains. Ref.1

Enzyme regulation

Inhibited by cellobiose. Ref.1

Subcellular location

Secreted Ref.1 Ref.2.

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Contains 1 CBM-cenC (cenC-type cellulose-binding) domain.

Contains 2 dockerin domains.

Biophysicochemical properties

Kinetic parameters:

KM=1.67 µM for PNP-cellobioside Ref.1

Vmax=15.1 µmol/min/mg enzyme

pH dependence:

Optimum pH is 6.0.

Temperature dependence:

Retains 97% of original activity when incubated for 200 hours at 60 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular space

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: InterPro

cellulose 1,4-beta-cellobiosidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.2
Chain28 – 895868Cellulose 1,4-beta-cellobiosidase
PRO_0000045748

Regions

Domain40 – 199160CBM-cenC
Domain834 – 85421Dockerin 1
Domain866 – 88621Dockerin 2
Region199 – 24042Linker
Region241 – 815575Catalytic

Sites

Active site7371 By similarity
Active site7861 By similarity
Active site7951 By similarity

Secondary structure

.............................. 895
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C2S1 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 5DB1FD84A6750CCE

FASTA895100,712
        10         20         30         40         50         60 
MNFRRMLCAA IVLTIVLSIM LPSTVFALED KSSKLPDYKN DLLYERTFDE GLCFPWHTCE 

        70         80         90        100        110        120 
DSGGKCDFAV VDVPGEPGNK AFRLTVIDKG QNKWSVQMRH RGITLEQGHT YTVRFTIWSD 

       130        140        150        160        170        180 
KSCRVYAKIG QMGEPYTEYW NNNWNPFNLT PGQKLTVEQN FTMNYPTDDT CEFTFHLGGE 

       190        200        210        220        230        240 
LAAGTPYYVY LDDVSLYDPR FVKPVEYVLP QPDVRVNQVG YLPFAKKYAT VVSSSTSPLK 

       250        260        270        280        290        300 
WQLLNSANQV VLEGNTIPKG LDKDSQDYVH WIDFSNFKTE GKGYYFKLPT VNSDTNYSHP 

       310        320        330        340        350        360 
FDISADIYSK MKFDALAFFY HKRSGIPIEM PYAGGEQWTR PAGHIGIEPN KGDTNVPTWP 

       370        380        390        400        410        420 
QDDEYAGRPQ KYYTKDVTGG WYDAGDHGKY VVNGGIAVWT LMNMYERAKI RGIANQGAYK 

       430        440        450        460        470        480 
DGGMNIPERN NGYPDILDEA RWEIEFFKKM QVTEKEDPSI AGMVHHKIHD FRWTALGMLP 

       490        500        510        520        530        540 
HEDPQPRYLR PVSTAATLNF AATLAQSARL WKDYDPTFAA DCLEKAEIAW QAALKHPDIY 

       550        560        570        580        590        600 
AEYTPGSGGP GGGPYNDDYV GDEFYWAACE LYVTTGKDEY KNYLMNSPHY LEMPAKMGEN 

       610        620        630        640        650        660 
GGANGEDNGL WGCFTWGTTQ GLGTITLALV ENGLPATDIQ KARNNIAKAA DRWLENIEEQ 

       670        680        690        700        710        720 
GYRLPIKQAE DERGGYPWGS NSFILNQMIV MGYAYDFTGN SKYLDGMQDG MSYLLGRNGL 

       730        740        750        760        770        780 
DQSYVTGYGE RPLQNPHDRF WTPQTSKKFP APPPGIIAGG PNSRFEDPTI TAAVKKDTPP 

       790        800        810        820        830        840 
QKCYIDHTDS WSTNEITVNW NAPFAWVTAY LDEIDLITPP GGVDPEEPEV IYGDCNGDGK 

       850        860        870        880        890 
VNSTDAVALK RYILRSGISI NTDNADVNAD GRVNSTDLAI LKRYILKEID VLPHK 

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References

[1]"Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination."
Kataeva I., Li X.L., Chen H., Choi S.-K., Ljungdahl L.G.
J. Bacteriol. 181:5288-5295(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 283-287 AND 326-337, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
Strain: JW20.
[2]"Dissociation of the cellulosome of Clostridium thermocellum in the presence of ethylenediaminetetraacetic acid occurs with the formation of trucated polypeptides."
Choi S.K., Ljungdahl L.G.
Biochemistry 35:4897-4905(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-45, SUBCELLULAR LOCATION.
Strain: JW20.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039030 Genomic DNA. Translation: AAC06139.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P6BX-ray2.00A/B27-210[»]
ProteinModelPortalP0C2S1.
SMRP0C2S1. Positions 208-813, 831-895.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR003305. CenC_carb-bd.
IPR018242. Dockerin_1.
IPR008979. Galactose-bd-like.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF02018. CBM_4_9. 1 hit.
PF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C2S1.

Entry information

Entry nameCELK_CLOTM
AccessionPrimary (citable) accession number: P0C2S1
Secondary accession number(s): O68438, Q10748, Q4CGG7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: October 16, 2013
This is version 32 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