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P0C2S5

- GUNS_CLOTM

UniProt

P0C2S5 - GUNS_CLOTM

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
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (17 Apr 2007)
      Previous versions | rss
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    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

    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-SubCell

    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 – 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.
    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

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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: October 1, 2014
    This is version 40 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