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P0C2S5

- GUNS_CLOTM

UniProt

P0C2S5 - GUNS_CLOTM

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Protein
Cellulose 1,4-beta-cellobiosidase (reducing end) CelS
Gene
celS
Organism
Clostridium thermocellum
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761Substrate
Active sitei87 – 871Proton donor1 Publication
Binding sitei140 – 1401Substrate
Binding sitei204 – 2041Substrate
Binding sitei241 – 2411Substrate
Binding sitei247 – 2471Substrate
Active sitei255 – 2551Nucleophile1 Publication
Binding sitei421 – 4211Substrate
Binding sitei520 – 5201Substrate
Metal bindingi679 – 6791Calcium 1
Metal bindingi681 – 6811Calcium 1
Metal bindingi683 – 6831Calcium 1
Metal bindingi684 – 6841Calcium 1; via amide nitrogen
Metal bindingi685 – 6851Calcium 1; via carbonyl oxygen
Metal bindingi690 – 6901Calcium 1
Metal bindingi711 – 7111Calcium 2
Metal bindingi711 – 7111Calcium 3
Metal bindingi712 – 7121Calcium 2; via amide nitrogen
Metal bindingi713 – 7131Calcium 3
Metal bindingi715 – 7151Calcium 3
Metal bindingi717 – 7171Calcium 2; via carbonyl oxygen
Metal bindingi717 – 7171Calcium 3; via carbonyl oxygen
Metal bindingi722 – 7221Calcium 2
Metal bindingi722 – 7221Calcium 3

GO - Molecular functioni

  1. cellulase activity Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH48. Glycoside Hydrolase Family 48.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:celS
OrganismiClostridium thermocellum
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 Publication
Add
BLAST
Chaini28 – 741714Cellulose 1,4-beta-cellobiosidase (reducing end) CelS
PRO_0000008027Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP0C2S5. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5213
Helixi54 – 563
Turni61 – 633
Beta strandi68 – 703
Beta strandi76 – 805
Beta strandi83 – 853
Helixi86 – 10318
Helixi107 – 11913
Helixi124 – 1263
Helixi130 – 1323
Helixi148 – 1503
Beta strandi152 – 1543
Turni157 – 1593
Helixi168 – 1758
Beta strandi184 – 1874
Beta strandi201 – 2044
Beta strandi214 – 2163
Beta strandi220 – 2245
Beta strandi226 – 2305
Helixi235 – 2384
Beta strandi247 – 2515
Helixi254 – 27320
Helixi277 – 2793
Helixi281 – 29313
Helixi294 – 2985
Beta strandi315 – 3173
Beta strandi329 – 3368
Beta strandi339 – 3424
Beta strandi345 – 3484
Helixi349 – 3513
Helixi354 – 3629
Helixi364 – 3663
Beta strandi369 – 3724
Helixi373 – 39119
Beta strandi394 – 3963
Beta strandi401 – 4066
Turni407 – 4104
Beta strandi423 – 4286
Turni432 – 4376
Helixi441 – 45717
Helixi460 – 4623
Helixi463 – 47412
Beta strandi485 – 49511
Beta strandi511 – 5188
Helixi521 – 54121
Beta strandi542 – 5443
Helixi547 – 56418
Beta strandi569 – 5724
Helixi579 – 5824
Helixi583 – 5864
Helixi611 – 6144
Helixi616 – 6205
Helixi624 – 6329
Helixi644 – 66017
Beta strandi680 – 6845
Helixi688 – 6903
Helixi691 – 6999
Helixi707 – 7093
Beta strandi712 – 7176
Helixi721 – 7299
Turni730 – 7356

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0C2S5.
SMRiP0C2S5. Positions 28-669, 673-741.

Miscellaneous databases

EvolutionaryTraceiP0C2S5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini679 – 69921Dockerin 1
Add
BLAST
Domaini711 – 73121Dockerin 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2522Substrate binding
Regioni301 – 3022Substrate binding
Regioni326 – 3272Substrate binding
Regioni645 – 6462Substrate binding

Domaini

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 similaritiesi

Contains 2 dockerin domains.

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProiIPR008928. 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]
PfamiPF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0C2S5-1 [UniParc]FASTAAdd to Basket

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MVKSRKISIL LAVAMLVSIM IPTTAFAGPT KAPTKDGTSY KDLFLELYGK    50
IKDPKNGYFS PDEGIPYHSI ETLIVEAPDY GHVTTSEAFS YYVWLEAMYG 100
NLTGNWSGVE TAWKVMEDWI IPDSTEQPGM SSYNPNSPAT YADEYEDPSY 150
YPSELKFDTV RVGSDPVHND LVSAYGPNMY LMHWLMDVDN WYGFGTGTRA 200
TFINTFQRGE QESTWETIPH PSIEEFKYGG PNGFLDLFTK DRSYAKQWRY 250
TNAPDAEGRA IQAVYWANKW AKEQGKGSAV ASVVSKAAKM GDFLRNDMFD 300
KYFMKIGAQD KTPATGYDSA HYLMAWYTAW GGGIGASWAW KIGCSHAHFG 350
YQNPFQGWVS ATQSDFAPKS SNGKRDWTTS YKRQLEFYQW LQSAEGGIAG 400
GATNSWNGRY EKYPAGTSTF YGMAYVPHPV YADPGSNQWF GFQAWSMQRV 450
MEYYLETGDS SVKNLIKKWV DWVMSEIKLY DDGTFAIPSD LEWSGQPDTW 500
TGTYTGNPNL HVRVTSYGTD LGVAGSLANA LATYAAATER WEGKLDTKAR 550
DMAAELVNRA WYNFYCSEGK GVVTEEARAD YKRFFEQEVY VPAGWSGTMP 600
NGDKIQPGIK FIDIRTKYRQ DPYYDIVYQA YLRGEAPVLN YHRFWHEVDL 650
AVAMGVLATY FPDMTYKVPG TPSTKLYGDV NDDGKVNSTD AVALKRYVLR 700
SGISINTDNA DLNEDGRVNS TDLGILKRYI LKEIDTLPYK N 741
Length:741
Mass (Da):83,558
Last modified:April 17, 2007 - v1
Checksum:i39FDF4680BDB1144
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DAQ NMR - A 673-741 [» ]
1DAV NMR - A 673-741 [» ]
1L1Y X-ray 2.40 A/B/C/D/E/F 1-678 [» ]
1L2A X-ray 2.50 A/B/C/D/E/F 1-678 [» ]
ProteinModelPortali P0C2S5.
SMRi P0C2S5. Positions 28-669, 673-741.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0C2S5. 1 interaction.

Protein family/group databases

CAZyi GH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C2S5.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 4 hits.
4.10.870.10. 1 hit.
InterProi IPR008928. 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 ]
Pfami PF00404. Dockerin_1. 2 hits.
PF02011. Glyco_hydro_48. 1 hit.
[Graphical view ]
PRINTSi PR00844. GLHYDRLASE48.
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGUNS_CLOTM
AccessioniPrimary (citable) accession number: P0C2S5
Secondary accession number(s): P38686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: September 3, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

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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