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P0C2S1

- CELK_CLOTM

UniProt

P0C2S1 - CELK_CLOTM

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Protein
Cellulose 1,4-beta-cellobiosidase
Gene
celK
Organism
Clostridium thermocellum
Status
Reviewed - 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

Vmax=15.1 µmol/min/mg enzyme

pH dependencei

Optimum pH is 6.0.

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei737 – 7371 By similarity
Active sitei786 – 7861 By similarity
Active sitei795 – 7951 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. 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
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 Publication
Add
BLAST
Chaini28 – 895868Cellulose 1,4-beta-cellobiosidase
PRO_0000045748Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 353
Helixi38 – 403
Beta strandi57 – 604
Beta strandi64 – 729
Beta strandi80 – 8910
Helixi93 – 953
Beta strandi96 – 10510
Beta strandi110 – 12112
Beta strandi123 – 13311
Beta strandi138 – 1425
Beta strandi147 – 1504
Beta strandi153 – 16210
Beta strandi168 – 1769
Helixi179 – 1813
Beta strandi184 – 19714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P6BX-ray2.00A/B27-210[»]
ProteinModelPortaliP0C2S1.
SMRiP0C2S1. Positions 208-813, 831-895.

Miscellaneous databases

EvolutionaryTraceiP0C2S1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 199160CBM-cenC
Add
BLAST
Domaini834 – 85421Dockerin 1
Add
BLAST
Domaini866 – 88621Dockerin 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 24042Linker
Add
BLAST
Regioni241 – 815575Catalytic
Add
BLAST

Sequence similaritiesi

Contains 2 dockerin domains.

Keywords - Domaini

Repeat, Signal

Family and domain databases

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.
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]
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.
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

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MNFRRMLCAA IVLTIVLSIM LPSTVFALED KSSKLPDYKN DLLYERTFDE    50
GLCFPWHTCE DSGGKCDFAV VDVPGEPGNK AFRLTVIDKG QNKWSVQMRH 100
RGITLEQGHT YTVRFTIWSD KSCRVYAKIG QMGEPYTEYW NNNWNPFNLT 150
PGQKLTVEQN FTMNYPTDDT CEFTFHLGGE LAAGTPYYVY LDDVSLYDPR 200
FVKPVEYVLP QPDVRVNQVG YLPFAKKYAT VVSSSTSPLK WQLLNSANQV 250
VLEGNTIPKG LDKDSQDYVH WIDFSNFKTE GKGYYFKLPT VNSDTNYSHP 300
FDISADIYSK MKFDALAFFY HKRSGIPIEM PYAGGEQWTR PAGHIGIEPN 350
KGDTNVPTWP QDDEYAGRPQ KYYTKDVTGG WYDAGDHGKY VVNGGIAVWT 400
LMNMYERAKI RGIANQGAYK DGGMNIPERN NGYPDILDEA RWEIEFFKKM 450
QVTEKEDPSI AGMVHHKIHD FRWTALGMLP HEDPQPRYLR PVSTAATLNF 500
AATLAQSARL WKDYDPTFAA DCLEKAEIAW QAALKHPDIY AEYTPGSGGP 550
GGGPYNDDYV GDEFYWAACE LYVTTGKDEY KNYLMNSPHY LEMPAKMGEN 600
GGANGEDNGL WGCFTWGTTQ GLGTITLALV ENGLPATDIQ KARNNIAKAA 650
DRWLENIEEQ GYRLPIKQAE DERGGYPWGS NSFILNQMIV MGYAYDFTGN 700
SKYLDGMQDG MSYLLGRNGL DQSYVTGYGE RPLQNPHDRF WTPQTSKKFP 750
APPPGIIAGG PNSRFEDPTI TAAVKKDTPP QKCYIDHTDS WSTNEITVNW 800
NAPFAWVTAY LDEIDLITPP GGVDPEEPEV IYGDCNGDGK VNSTDAVALK 850
RYILRSGISI NTDNADVNAD GRVNSTDLAI LKRYILKEID VLPHK 895
Length:895
Mass (Da):100,712
Last modified:April 17, 2007 - v1
Checksum:i5DB1FD84A6750CCE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF039030 Genomic DNA. Translation: AAC06139.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF039030 Genomic DNA. Translation: AAC06139.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3P6B X-ray 2.00 A/B 27-210 [» ]
ProteinModelPortali P0C2S1.
SMRi P0C2S1. Positions 208-813, 831-895.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM4. Carbohydrate-Binding Module Family 4.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C2S1.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProi IPR008928. 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 ]
Pfami PF02018. CBM_4_9. 1 hit.
PF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: September 3, 2014
This is version 33 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

External Data

Dasty 3

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