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Protein

Cellulose 1,4-beta-cellobiosidase (reducing end) CelS

Gene

celS

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei76Substrate1 Publication1
Active sitei87Proton donor1 Publication1
Binding sitei140Substrate1 Publication1
Binding sitei204Substrate1 Publication1
Binding sitei241Substrate1 Publication1
Binding sitei247Substrate1 Publication1
Active sitei255Nucleophile1 Publication1
Binding sitei421Substrate1 Publication1
Binding sitei520Substrate1 Publication1
Metal bindingi679Calcium 11 Publication1
Metal bindingi681Calcium 11 Publication1
Metal bindingi683Calcium 11 Publication1
Metal bindingi684Calcium 1; via amide nitrogen1 Publication1
Metal bindingi685Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi690Calcium 11 Publication1
Metal bindingi711Calcium 21 Publication1
Metal bindingi711Calcium 31 Publication1
Metal bindingi712Calcium 2; via amide nitrogen1 Publication1
Metal bindingi713Calcium 31 Publication1
Metal bindingi715Calcium 31 Publication1
Metal bindingi717Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi717Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi722Calcium 21 Publication1
Metal bindingi722Calcium 31 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.176. 1530.

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 (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000000802728 – 741Cellulose 1,4-beta-cellobiosidase (reducing end) CelSAdd BLAST714

Interactioni

Protein-protein interaction databases

IntActiP0C2S5. 1 interactor.
STRINGi203119.Cthe_2089.

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 52Combined sources13
Helixi54 – 56Combined sources3
Turni61 – 63Combined sources3
Beta strandi68 – 70Combined sources3
Beta strandi76 – 80Combined sources5
Beta strandi83 – 85Combined sources3
Helixi86 – 103Combined sources18
Helixi107 – 119Combined sources13
Helixi124 – 126Combined sources3
Helixi130 – 132Combined sources3
Helixi148 – 150Combined sources3
Beta strandi152 – 154Combined sources3
Turni157 – 159Combined sources3
Helixi168 – 175Combined sources8
Beta strandi184 – 187Combined sources4
Beta strandi201 – 204Combined sources4
Beta strandi214 – 216Combined sources3
Beta strandi220 – 224Combined sources5
Beta strandi226 – 230Combined sources5
Helixi235 – 238Combined sources4
Beta strandi247 – 251Combined sources5
Helixi254 – 273Combined sources20
Helixi277 – 279Combined sources3
Helixi281 – 293Combined sources13
Helixi294 – 298Combined sources5
Beta strandi315 – 317Combined sources3
Beta strandi329 – 336Combined sources8
Beta strandi339 – 342Combined sources4
Beta strandi345 – 348Combined sources4
Helixi349 – 351Combined sources3
Helixi354 – 362Combined sources9
Helixi364 – 366Combined sources3
Beta strandi369 – 372Combined sources4
Helixi373 – 391Combined sources19
Beta strandi394 – 396Combined sources3
Beta strandi401 – 406Combined sources6
Turni407 – 410Combined sources4
Beta strandi423 – 428Combined sources6
Turni432 – 437Combined sources6
Helixi441 – 457Combined sources17
Helixi460 – 462Combined sources3
Helixi463 – 474Combined sources12
Beta strandi485 – 495Combined sources11
Beta strandi511 – 518Combined sources8
Helixi521 – 541Combined sources21
Beta strandi542 – 544Combined sources3
Helixi547 – 564Combined sources18
Beta strandi569 – 572Combined sources4
Helixi579 – 582Combined sources4
Helixi583 – 586Combined sources4
Helixi611 – 614Combined sources4
Helixi616 – 620Combined sources5
Helixi624 – 632Combined sources9
Helixi644 – 660Combined sources17
Beta strandi680 – 684Combined sources5
Helixi688 – 690Combined sources3
Helixi691 – 699Combined sources9
Helixi707 – 709Combined sources3
Beta strandi712 – 717Combined sources6
Helixi721 – 729Combined sources9
Turni730 – 735Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MTENMR-A673-741[»]
ProteinModelPortaliP0C2S5.
SMRiP0C2S5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2S5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini673 – 739DockerinPROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni251 – 252Substrate binding2
Regioni301 – 302Substrate binding2
Regioni326 – 327Substrate binding2
Regioni645 – 646Substrate binding2

Sequence similaritiesi

Contains 1 dockerin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
ENOG410XPC9. LUCA.

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.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
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.
PS51766. DOCKERIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0C2S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKSRKISIL LAVAMLVSIM IPTTAFAGPT KAPTKDGTSY KDLFLELYGK
60 70 80 90 100
IKDPKNGYFS PDEGIPYHSI ETLIVEAPDY GHVTTSEAFS YYVWLEAMYG
110 120 130 140 150
NLTGNWSGVE TAWKVMEDWI IPDSTEQPGM SSYNPNSPAT YADEYEDPSY
160 170 180 190 200
YPSELKFDTV RVGSDPVHND LVSAYGPNMY LMHWLMDVDN WYGFGTGTRA
210 220 230 240 250
TFINTFQRGE QESTWETIPH PSIEEFKYGG PNGFLDLFTK DRSYAKQWRY
260 270 280 290 300
TNAPDAEGRA IQAVYWANKW AKEQGKGSAV ASVVSKAAKM GDFLRNDMFD
310 320 330 340 350
KYFMKIGAQD KTPATGYDSA HYLMAWYTAW GGGIGASWAW KIGCSHAHFG
360 370 380 390 400
YQNPFQGWVS ATQSDFAPKS SNGKRDWTTS YKRQLEFYQW LQSAEGGIAG
410 420 430 440 450
GATNSWNGRY EKYPAGTSTF YGMAYVPHPV YADPGSNQWF GFQAWSMQRV
460 470 480 490 500
MEYYLETGDS SVKNLIKKWV DWVMSEIKLY DDGTFAIPSD LEWSGQPDTW
510 520 530 540 550
TGTYTGNPNL HVRVTSYGTD LGVAGSLANA LATYAAATER WEGKLDTKAR
560 570 580 590 600
DMAAELVNRA WYNFYCSEGK GVVTEEARAD YKRFFEQEVY VPAGWSGTMP
610 620 630 640 650
NGDKIQPGIK FIDIRTKYRQ DPYYDIVYQA YLRGEAPVLN YHRFWHEVDL
660 670 680 690 700
AVAMGVLATY FPDMTYKVPG TPSTKLYGDV NDDGKVNSTD AVALKRYVLR
710 720 730 740
SGISINTDNA DLNEDGRVNS TDLGILKRYI LKEIDTLPYK N
Length:741
Mass (Da):83,558
Last modified:April 17, 2007 - v1
Checksum:i39FDF4680BDB1144
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MTENMR-A673-741[»]
ProteinModelPortaliP0C2S5.
SMRiP0C2S5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C2S5. 1 interactor.
STRINGi203119.Cthe_2089.

Protein family/group databases

CAZyiGH48. Glycoside Hydrolase Family 48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
ENOG410XPC9. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.176. 1530.

Miscellaneous databases

EvolutionaryTraceiP0C2S5.

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.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
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.
PS51766. DOCKERIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 51 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.Curated

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.