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P0C2S5 (GUNS_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 38. 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 (reducing end) CelS

EC=3.2.1.176
Alternative name(s):
Cellobiohydrolase CelS
Cellulase SS
Endo-1,4-beta-glucanase
Endoglucanase SS
Short name=EGSS
Exocellulase
Gene names
Name:celS
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose. Ref.3

Catalytic activity

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains. Ref.3

Enzyme regulation

Inhibited by cellobiose and lactose, but not by glucose By similarity.

Subcellular location

Secreted.

Domain

The dockerin domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similarities

Belongs to the glycosyl hydrolase 48 (cellulase L) family.

Contains 2 dockerin domains.

Caution

The N-terminal sequence shown here has been extracted from PDB entry 1L1Y.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 741714Cellulose 1,4-beta-cellobiosidase (reducing end) CelS
PRO_0000008027

Regions

Domain679 – 69921Dockerin 1
Domain711 – 73121Dockerin 2
Region251 – 2522Substrate binding
Region301 – 3022Substrate binding
Region326 – 3272Substrate binding
Region645 – 6462Substrate binding

Sites

Active site871Proton donor Ref.3
Active site2551Nucleophile Ref.3
Metal binding6791Calcium 1
Metal binding6811Calcium 1
Metal binding6831Calcium 1
Metal binding6841Calcium 1; via amide nitrogen
Metal binding6851Calcium 1; via carbonyl oxygen
Metal binding6901Calcium 1
Metal binding7111Calcium 2
Metal binding7111Calcium 3
Metal binding7121Calcium 2; via amide nitrogen
Metal binding7131Calcium 3
Metal binding7151Calcium 3
Metal binding7171Calcium 2; via carbonyl oxygen
Metal binding7171Calcium 3; via carbonyl oxygen
Metal binding7221Calcium 2
Metal binding7221Calcium 3
Binding site761Substrate
Binding site1401Substrate
Binding site2041Substrate
Binding site2411Substrate
Binding site2471Substrate
Binding site4211Substrate
Binding site5201Substrate

Secondary structure

................................................................................................................. 741
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C2S5 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 39FDF4680BDB1144

FASTA74183,558
        10         20         30         40         50         60 
MVKSRKISIL LAVAMLVSIM IPTTAFAGPT KAPTKDGTSY KDLFLELYGK IKDPKNGYFS 

        70         80         90        100        110        120 
PDEGIPYHSI ETLIVEAPDY GHVTTSEAFS YYVWLEAMYG NLTGNWSGVE TAWKVMEDWI 

       130        140        150        160        170        180 
IPDSTEQPGM SSYNPNSPAT YADEYEDPSY YPSELKFDTV RVGSDPVHND LVSAYGPNMY 

       190        200        210        220        230        240 
LMHWLMDVDN WYGFGTGTRA TFINTFQRGE QESTWETIPH PSIEEFKYGG PNGFLDLFTK 

       250        260        270        280        290        300 
DRSYAKQWRY TNAPDAEGRA IQAVYWANKW AKEQGKGSAV ASVVSKAAKM GDFLRNDMFD 

       310        320        330        340        350        360 
KYFMKIGAQD KTPATGYDSA HYLMAWYTAW GGGIGASWAW KIGCSHAHFG YQNPFQGWVS 

       370        380        390        400        410        420 
ATQSDFAPKS SNGKRDWTTS YKRQLEFYQW LQSAEGGIAG GATNSWNGRY EKYPAGTSTF 

       430        440        450        460        470        480 
YGMAYVPHPV YADPGSNQWF GFQAWSMQRV MEYYLETGDS SVKNLIKKWV DWVMSEIKLY 

       490        500        510        520        530        540 
DDGTFAIPSD LEWSGQPDTW TGTYTGNPNL HVRVTSYGTD LGVAGSLANA LATYAAATER 

       550        560        570        580        590        600 
WEGKLDTKAR DMAAELVNRA WYNFYCSEGK GVVTEEARAD YKRFFEQEVY VPAGWSGTMP 

       610        620        630        640        650        660 
NGDKIQPGIK FIDIRTKYRQ DPYYDIVYQA YLRGEAPVLN YHRFWHEVDL AVAMGVLATY 

       670        680        690        700        710        720 
FPDMTYKVPG TPSTKLYGDV NDDGKVNSTD AVALKRYVLR SGISINTDNA DLNEDGRVNS 

       730        740 
TDLGILKRYI LKEIDTLPYK N 

« Hide

References

[1]"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 28-46 AND 674-741.
Strain: JW20.
[2]"Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain."
Lytle B.L., Volkman B.F., Westler W.M., Heckman M.P., Wu J.H.
J. Mol. Biol. 307:745-753(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 673-741 IN COMPLEX WITH CALCIUM.
[3]"Catalytic mechanism of cellulose degradation by a cellobiohydrolase, CelS."
Saharay M., Guo H., Smith J.C.
PLoS ONE 5:E12947-E12947(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE.
[4]"The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome."
Guimaraes B.G., Souchon H., Lytle B.L., David Wu J.H., Alzari P.M.
J. Mol. Biol. 320:587-596(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-678 IN COMPLEX WITH SUBSTRATE.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DAQNMR-A673-741[»]
1DAVNMR-A673-741[»]
1L1YX-ray2.40A/B/C/D/E/F1-678[»]
1L2AX-ray2.50A/B/C/D/E/F1-678[»]
ProteinModelPortalP0C2S5.
SMRP0C2S5. Positions 28-669, 673-741.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0C2S5. 1 interaction.

Protein family/group databases

CAZyGH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
[Graphical view]
PfamPF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSPR00844. GLHYDRLASE48.
SUPFAMSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C2S5.

Entry information

Entry nameGUNS_CLOTM
AccessionPrimary (citable) accession number: P0C2S5
Secondary accession number(s): P38686
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: December 11, 2013
This is version 38 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