GUNS_ACETH
ID GUNS_ACETH Reviewed; 741 AA.
AC P0C2S5; P38686;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Cellulose 1,4-beta-cellobiosidase (reducing end) CelS;
DE EC=3.2.1.176;
DE AltName: Full=Cellobiohydrolase CelS;
DE AltName: Full=Cellulase SS;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE AltName: Full=Endoglucanase SS;
DE Short=EGSS;
DE AltName: Full=Exocellulase;
DE Flags: Precursor;
GN Name=celS;
OS Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1515;
RN [1]
RP PROTEIN SEQUENCE OF 28-46 AND 674-741.
RC STRAIN=JW20;
RX PubMed=8664281; DOI=10.1021/bi9524629;
RA Choi S.K., Ljungdahl L.G.;
RT "Dissociation of the cellulosome of Clostridium thermocellum in the
RT presence of ethylenediaminetetraacetic acid occurs with the formation of
RT trucated polypeptides.";
RL Biochemistry 35:4897-4905(1996).
RN [2]
RP STRUCTURE BY NMR OF 673-741 IN COMPLEX WITH CALCIUM.
RX PubMed=11273698; DOI=10.1006/jmbi.2001.4522;
RA Lytle B.L., Volkman B.F., Westler W.M., Heckman M.P., Wu J.H.;
RT "Solution structure of a type I dockerin domain, a novel prokaryotic,
RT extracellular calcium-binding domain.";
RL J. Mol. Biol. 307:745-753(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=20967294; DOI=10.1371/journal.pone.0012947;
RA Saharay M., Guo H., Smith J.C.;
RT "Catalytic mechanism of cellulose degradation by a cellobiohydrolase,
RT CelS.";
RL PLoS ONE 5:E12947-E12947(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-678 IN COMPLEX WITH SUBSTRATE.
RX PubMed=12096911; DOI=10.1016/s0022-2836(02)00497-7;
RA Guimaraes B.G., Souchon H., Lytle B.L., David Wu J.H., Alzari P.M.;
RT "The crystal structure and catalytic mechanism of cellobiohydrolase CelS,
RT the major enzymatic component of the Clostridium thermocellum
RT Cellulosome.";
RL J. Mol. Biol. 320:587-596(2002).
CC -!- FUNCTION: This enzyme catalyzes the exohydrolysis of 1,4-beta-
CC glucosidic linkages in cellulose with a preference for amorphous or
CC crystalline cellulose over carboxymethyl cellulose.
CC {ECO:0000269|PubMed:20967294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and similar substrates, releasing cellobiose from the reducing ends
CC of the chains.; EC=3.2.1.176; Evidence={ECO:0000269|PubMed:20967294};
CC -!- ACTIVITY REGULATION: Inhibited by cellobiose and lactose, but not by
CC glucose. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 48 (cellulase L) family.
CC {ECO:0000305}.
CC -!- CAUTION: The N-terminal sequence shown here has been extracted from PDB
CC entry 1L1Y. {ECO:0000305}.
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DR PDB; 1DAQ; NMR; -; A=673-741.
DR PDB; 1DAV; NMR; -; A=673-741.
DR PDB; 1L1Y; X-ray; 2.40 A; A/B/C/D/E/F=1-678.
DR PDB; 1L2A; X-ray; 2.50 A; A/B/C/D/E/F=1-678.
DR PDB; 2MTE; NMR; -; A=673-741.
DR PDBsum; 1DAQ; -.
DR PDBsum; 1DAV; -.
DR PDBsum; 1L1Y; -.
DR PDBsum; 1L2A; -.
DR PDBsum; 2MTE; -.
DR AlphaFoldDB; P0C2S5; -.
DR BMRB; P0C2S5; -.
DR SMR; P0C2S5; -.
DR IntAct; P0C2S5; 1.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; GH48; Glycoside Hydrolase Family 48.
DR BRENDA; 3.2.1.176; 1530.
DR EvolutionaryTrace; P0C2S5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0102252; F:cellulose 1,4-beta-cellobiosidase activity (reducing end); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.170.160.10; -; 1.
DR Gene3D; 4.10.870.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR InterPro; IPR027390; Endoglucanase_F_dom3.
DR InterPro; IPR000556; Glyco_hydro_48F.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF02011; Glyco_hydro_48; 1.
DR PRINTS; PR00844; GLHYDRLASE48.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:8664281"
FT CHAIN 28..741
FT /note="Cellulose 1,4-beta-cellobiosidase (reducing end)
FT CelS"
FT /id="PRO_0000008027"
FT DOMAIN 673..739
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT ACT_SITE 87
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:20967294"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:20967294"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12096911"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12096911"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12096911"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12096911"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12096911"
FT BINDING 251..252
FT /ligand="substrate"
FT BINDING 301..302
FT /ligand="substrate"
FT BINDING 326..327
FT /ligand="substrate"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12096911"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12096911"
FT BINDING 645..646
FT /ligand="substrate"
FT BINDING 679
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 681
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 683
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 684
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 685
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 690
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 712
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 713
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 715
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 717
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 717
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11273698"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11273698"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1L1Y"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 86..103
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1L2A"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1L1Y"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 254..273
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 373..391
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:1L1Y"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:1L1Y"
FT TURN 432..437
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 441..457
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 463..474
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 485..495
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 511..518
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 521..541
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 547..564
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 579..582
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 611..614
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 616..620
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 624..632
FT /evidence="ECO:0007829|PDB:1L1Y"
FT HELIX 644..660
FT /evidence="ECO:0007829|PDB:1L1Y"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:1DAQ"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:1DAQ"
FT HELIX 691..699
FT /evidence="ECO:0007829|PDB:1DAQ"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:1DAQ"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:1DAQ"
FT HELIX 721..729
FT /evidence="ECO:0007829|PDB:1DAQ"
FT TURN 730..735
FT /evidence="ECO:0007829|PDB:1DAQ"
SQ SEQUENCE 741 AA; 83558 MW; 39FDF4680BDB1144 CRC64;
MVKSRKISIL LAVAMLVSIM IPTTAFAGPT KAPTKDGTSY KDLFLELYGK IKDPKNGYFS
PDEGIPYHSI ETLIVEAPDY GHVTTSEAFS YYVWLEAMYG NLTGNWSGVE TAWKVMEDWI
IPDSTEQPGM SSYNPNSPAT YADEYEDPSY YPSELKFDTV RVGSDPVHND LVSAYGPNMY
LMHWLMDVDN WYGFGTGTRA TFINTFQRGE QESTWETIPH PSIEEFKYGG PNGFLDLFTK
DRSYAKQWRY TNAPDAEGRA IQAVYWANKW AKEQGKGSAV ASVVSKAAKM GDFLRNDMFD
KYFMKIGAQD KTPATGYDSA HYLMAWYTAW GGGIGASWAW KIGCSHAHFG YQNPFQGWVS
ATQSDFAPKS SNGKRDWTTS YKRQLEFYQW LQSAEGGIAG GATNSWNGRY EKYPAGTSTF
YGMAYVPHPV YADPGSNQWF GFQAWSMQRV MEYYLETGDS SVKNLIKKWV DWVMSEIKLY
DDGTFAIPSD LEWSGQPDTW TGTYTGNPNL HVRVTSYGTD LGVAGSLANA LATYAAATER
WEGKLDTKAR DMAAELVNRA WYNFYCSEGK GVVTEEARAD YKRFFEQEVY VPAGWSGTMP
NGDKIQPGIK FIDIRTKYRQ DPYYDIVYQA YLRGEAPVLN YHRFWHEVDL AVAMGVLATY
FPDMTYKVPG TPSTKLYGDV NDDGKVNSTD AVALKRYVLR SGISINTDNA DLNEDGRVNS
TDLGILKRYI LKEIDTLPYK N
