GUNS_ACET2
ID GUNS_ACET2 Reviewed; 741 AA.
AC A3DH67; P38686;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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; OrderedLocusNames=Cthe_2089;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-37; 412-431
RP AND 589-605.
RX PubMed=8444792; DOI=10.1128/jb.175.5.1293-1302.1993;
RA Wang W.K., Kruus K., Wu J.H.D.;
RT "Cloning and DNA sequence of the gene coding for Clostridium thermocellum
RT cellulase Ss (CelS), a major cellulosome component.";
RL J. Bacteriol. 175:1293-1302(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ACTIVITY REGULATION.
RX PubMed=8597541; DOI=10.1007/bf00169935;
RA Kruus K., Andreacchi A., Wang W.K., Wu J.H.D.;
RT "Product inhibition of the recombinant CelS, an exoglucanase component of
RT the Clostridium thermocellum cellulosome.";
RL Appl. Microbiol. Biotechnol. 44:399-404(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7883725; DOI=10.1128/jb.177.6.1641-1644.1995;
RA Kruus K., Wang W.K., Ching J., Wu J.H.;
RT "Exoglucanase activities of the recombinant Clostridium thermocellum CelS,
RT a major cellulosome component.";
RL J. Bacteriol. 177:1641-1644(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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:7883725}.
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:7883725};
CC -!- ACTIVITY REGULATION: Inhibited by cellobiose and lactose, but not by
CC glucose. {ECO:0000269|PubMed:8597541}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-6. {ECO:0000269|PubMed:7883725};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:7883725};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 48 (cellulase L) family.
CC {ECO:0000305}.
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DR EMBL; L06942; AAA23226.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN53296.1; -; Genomic_DNA.
DR PIR; A47063; A47063.
DR AlphaFoldDB; A3DH67; -.
DR BMRB; A3DH67; -.
DR SMR; A3DH67; -.
DR STRING; 203119.Cthe_2089; -.
DR CAZy; GH48; Glycoside Hydrolase Family 48.
DR EnsemblBacteria; ABN53296; ABN53296; Cthe_2089.
DR KEGG; cth:Cthe_2089; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_009014_1_0_9; -.
DR OMA; QWFGFQA; -.
DR BioCyc; MetaCyc:MON-16423; -.
DR BRENDA; 3.2.1.176; 1530.
DR Proteomes; UP000002145; Chromosome.
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 Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:8444792"
FT CHAIN 28..741
FT /note="Cellulose 1,4-beta-cellobiosidase (reducing end)
FT CelS"
FT /id="PRO_0000284723"
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:0000250"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251..252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301..302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326..327
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 645..646
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 679
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 681
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 683
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 690
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 712
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 713
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 715
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 717
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 717
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
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
