Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cellulose 1,4-beta-cellobiosidase

Gene

celK

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Inhibited by cellobiose.1 Publication

Kineticsi

  1. KM=1.67 µM for PNP-cellobioside1 Publication
  1. Vmax=15.1 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

Retains 97% of original activity when incubated for 200 hours at 60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei737By similarity1
Active sitei786By similarity1
Active sitei795By similarity1

GO - Molecular functioni

  • cellulase activity Source: InterPro
  • cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB

GO - Biological processi

  • polysaccharide catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiCBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose 1,4-beta-cellobiosidase (EC:3.2.1.91)
Gene namesi
Name:celK
OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Subcellular locationi

  • Secreted 2 Publications

GO - Cellular componenti

  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000004574828 – 895Cellulose 1,4-beta-cellobiosidaseAdd BLAST868

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_0412.

Structurei

Secondary structure

1895
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 35Combined sources3
Helixi38 – 40Combined sources3
Beta strandi57 – 60Combined sources4
Beta strandi64 – 72Combined sources9
Beta strandi80 – 89Combined sources10
Helixi93 – 95Combined sources3
Beta strandi96 – 105Combined sources10
Beta strandi110 – 121Combined sources12
Beta strandi123 – 133Combined sources11
Beta strandi138 – 142Combined sources5
Beta strandi147 – 150Combined sources4
Beta strandi153 – 162Combined sources10
Beta strandi168 – 176Combined sources9
Helixi179 – 181Combined sources3
Beta strandi184 – 197Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P6BX-ray2.00A/B27-210[»]
ProteinModelPortaliP0C2S1.
SMRiP0C2S1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2S1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 199CBM-cenCAdd BLAST160
Domaini828 – 894DockerinPROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 240LinkerAdd BLAST42
Regioni241 – 815CatalyticAdd BLAST575

Sequence similaritiesi

Contains 1 dockerin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E08. Bacteria.
ENOG410XNTA. LUCA.

Family and domain databases

CDDicd02850. E_set_Cellulase_N. 1 hit.
Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR004197. Cellulase_Ig-like.
IPR003305. CenC_carb-bd.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR008979. Galactose-bd-like.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF02018. CBM_4_9. 1 hit.
PF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS51766. DOCKERIN. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C2S1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFRRMLCAA IVLTIVLSIM LPSTVFALED KSSKLPDYKN DLLYERTFDE
60 70 80 90 100
GLCFPWHTCE DSGGKCDFAV VDVPGEPGNK AFRLTVIDKG QNKWSVQMRH
110 120 130 140 150
RGITLEQGHT YTVRFTIWSD KSCRVYAKIG QMGEPYTEYW NNNWNPFNLT
160 170 180 190 200
PGQKLTVEQN FTMNYPTDDT CEFTFHLGGE LAAGTPYYVY LDDVSLYDPR
210 220 230 240 250
FVKPVEYVLP QPDVRVNQVG YLPFAKKYAT VVSSSTSPLK WQLLNSANQV
260 270 280 290 300
VLEGNTIPKG LDKDSQDYVH WIDFSNFKTE GKGYYFKLPT VNSDTNYSHP
310 320 330 340 350
FDISADIYSK MKFDALAFFY HKRSGIPIEM PYAGGEQWTR PAGHIGIEPN
360 370 380 390 400
KGDTNVPTWP QDDEYAGRPQ KYYTKDVTGG WYDAGDHGKY VVNGGIAVWT
410 420 430 440 450
LMNMYERAKI RGIANQGAYK DGGMNIPERN NGYPDILDEA RWEIEFFKKM
460 470 480 490 500
QVTEKEDPSI AGMVHHKIHD FRWTALGMLP HEDPQPRYLR PVSTAATLNF
510 520 530 540 550
AATLAQSARL WKDYDPTFAA DCLEKAEIAW QAALKHPDIY AEYTPGSGGP
560 570 580 590 600
GGGPYNDDYV GDEFYWAACE LYVTTGKDEY KNYLMNSPHY LEMPAKMGEN
610 620 630 640 650
GGANGEDNGL WGCFTWGTTQ GLGTITLALV ENGLPATDIQ KARNNIAKAA
660 670 680 690 700
DRWLENIEEQ GYRLPIKQAE DERGGYPWGS NSFILNQMIV MGYAYDFTGN
710 720 730 740 750
SKYLDGMQDG MSYLLGRNGL DQSYVTGYGE RPLQNPHDRF WTPQTSKKFP
760 770 780 790 800
APPPGIIAGG PNSRFEDPTI TAAVKKDTPP QKCYIDHTDS WSTNEITVNW
810 820 830 840 850
NAPFAWVTAY LDEIDLITPP GGVDPEEPEV IYGDCNGDGK VNSTDAVALK
860 870 880 890
RYILRSGISI NTDNADVNAD GRVNSTDLAI LKRYILKEID VLPHK
Length:895
Mass (Da):100,712
Last modified:April 17, 2007 - v1
Checksum:i5DB1FD84A6750CCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039030 Genomic DNA. Translation: AAC06139.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039030 Genomic DNA. Translation: AAC06139.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P6BX-ray2.00A/B27-210[»]
ProteinModelPortaliP0C2S1.
SMRiP0C2S1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203119.Cthe_0412.

Protein family/group databases

CAZyiCBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105E08. Bacteria.
ENOG410XNTA. LUCA.

Miscellaneous databases

EvolutionaryTraceiP0C2S1.

Family and domain databases

CDDicd02850. E_set_Cellulase_N. 1 hit.
Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR004197. Cellulase_Ig-like.
IPR003305. CenC_carb-bd.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR008979. Galactose-bd-like.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF02018. CBM_4_9. 1 hit.
PF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS51766. DOCKERIN. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCELK_CLOTM
AccessioniPrimary (citable) accession number: P0C2S1
Secondary accession number(s): O68438, Q10748, Q4CGG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.