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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 (Ruminiclostridium 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 – 761Substrate1 Publication
Active sitei87 – 871Proton donor1 Publication
Binding sitei140 – 1401Substrate1 Publication
Binding sitei204 – 2041Substrate1 Publication
Binding sitei241 – 2411Substrate1 Publication
Binding sitei247 – 2471Substrate1 Publication
Active sitei255 – 2551Nucleophile1 Publication
Binding sitei421 – 4211Substrate1 Publication
Binding sitei520 – 5201Substrate1 Publication
Metal bindingi679 – 6791Calcium 11 Publication
Metal bindingi681 – 6811Calcium 11 Publication
Metal bindingi683 – 6831Calcium 11 Publication
Metal bindingi684 – 6841Calcium 1; via amide nitrogen1 Publication
Metal bindingi685 – 6851Calcium 1; via carbonyl oxygen1 Publication
Metal bindingi690 – 6901Calcium 11 Publication
Metal bindingi711 – 7111Calcium 21 Publication
Metal bindingi711 – 7111Calcium 31 Publication
Metal bindingi712 – 7121Calcium 2; via amide nitrogen1 Publication
Metal bindingi713 – 7131Calcium 31 Publication
Metal bindingi715 – 7151Calcium 31 Publication
Metal bindingi717 – 7171Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi717 – 7171Calcium 3; via carbonyl oxygen1 Publication
Metal bindingi722 – 7221Calcium 21 Publication
Metal bindingi722 – 7221Calcium 31 Publication

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 (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 741714Cellulose 1,4-beta-cellobiosidase (reducing end) CelSPRO_0000008027Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP0C2S5. 1 interaction.

Structurei

Secondary structure

1
741
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5213Combined sources
Helixi54 – 563Combined sources
Turni61 – 633Combined sources
Beta strandi68 – 703Combined sources
Beta strandi76 – 805Combined sources
Beta strandi83 – 853Combined sources
Helixi86 – 10318Combined sources
Helixi107 – 11913Combined sources
Helixi124 – 1263Combined sources
Helixi130 – 1323Combined sources
Helixi148 – 1503Combined sources
Beta strandi152 – 1543Combined sources
Turni157 – 1593Combined sources
Helixi168 – 1758Combined sources
Beta strandi184 – 1874Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi226 – 2305Combined sources
Helixi235 – 2384Combined sources
Beta strandi247 – 2515Combined sources
Helixi254 – 27320Combined sources
Helixi277 – 2793Combined sources
Helixi281 – 29313Combined sources
Helixi294 – 2985Combined sources
Beta strandi315 – 3173Combined sources
Beta strandi329 – 3368Combined sources
Beta strandi339 – 3424Combined sources
Beta strandi345 – 3484Combined sources
Helixi349 – 3513Combined sources
Helixi354 – 3629Combined sources
Helixi364 – 3663Combined sources
Beta strandi369 – 3724Combined sources
Helixi373 – 39119Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi401 – 4066Combined sources
Turni407 – 4104Combined sources
Beta strandi423 – 4286Combined sources
Turni432 – 4376Combined sources
Helixi441 – 45717Combined sources
Helixi460 – 4623Combined sources
Helixi463 – 47412Combined sources
Beta strandi485 – 49511Combined sources
Beta strandi511 – 5188Combined sources
Helixi521 – 54121Combined sources
Beta strandi542 – 5443Combined sources
Helixi547 – 56418Combined sources
Beta strandi569 – 5724Combined sources
Helixi579 – 5824Combined sources
Helixi583 – 5864Combined sources
Helixi611 – 6144Combined sources
Helixi616 – 6205Combined sources
Helixi624 – 6329Combined sources
Helixi644 – 66017Combined sources
Beta strandi680 – 6845Combined sources
Helixi688 – 6903Combined sources
Helixi691 – 6999Combined sources
Helixi707 – 7093Combined sources
Beta strandi712 – 7176Combined sources
Helixi721 – 7299Combined sources
Turni730 – 7356Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2S5.

Family & Domainsi

Domains and Repeats

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

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

« 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
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: November 26, 2014
This is version 42 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

External Data

Dasty 3