ID   CELK_ACET2              Reviewed;         895 AA.
AC   A3DCH1; O68438; Q10748; Q4CGG7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Cellulose 1,4-beta-cellobiosidase;
DE            EC=3.2.1.91;
DE   Flags: Precursor;
GN   Name=celK; OrderedLocusNames=Cthe_0412; ORFNames=CtheDRAFT_2165;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 /
RC   NRRL 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC         and cellotetraose, releasing cellobiose from the non-reducing ends of
CC         the chains.; EC=3.2.1.91;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR   EMBL; CP000568; ABN51650.1; -; Genomic_DNA.
DR   RefSeq; WP_011837826.1; NC_009012.1.
DR   AlphaFoldDB; A3DCH1; -.
DR   SMR; A3DCH1; -.
DR   STRING; 203119.Cthe_0412; -.
DR   CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   KEGG; cth:Cthe_0412; -.
DR   eggNOG; COG2273; Bacteria.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_006010_0_0_9; -.
DR   OrthoDB; 9758662at2; -.
DR   BioCyc; MetaCyc:MONOMER-16421; -.
DR   BRENDA; 3.2.1.91; 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:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14256; Dockerin_I; 1.
DR   CDD; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..895
FT                   /note="Cellulose 1,4-beta-cellobiosidase"
FT                   /id="PRO_0000284718"
FT   DOMAIN          40..199
FT                   /note="CBM-cenC"
FT   DOMAIN          828..894
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   REGION          199..240
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          241..815
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        386
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        737
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        786
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        795
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   895 AA;  100622 MW;  9354DFE9EC75BE67 CRC64;
     MNFRRMLCAA IVLTIVLSIM LPSTVFALED KSPKLPDYKN DLLYERTFDE GLCFPWHTCE
     DSGGKCDFAV VDVPGEPGNK AFRLTVIDKG QNKWSVQMRH RGITLEQGHT YTVRFTIWSD
     KSCRVYAKIG QMGEPYTEYW NNNWNPFNLT PGQKLTVEQN FTMNYPTDDT CEFTFHLGGE
     LAAGTPYYVY LDDVSLYDPR FVKPVEYVLP QPDVRVNQVG YLPFAKKYAT VVSSSTSPLK
     WQLLNSANQV VLEGNTIPKG LDKDSQDYVH WIDFSNFKTE GKGYYFKLPT VNSDTNYSHP
     FDISADIYSK MKFDALAFFY HKRSGIPIEM PYAGGEQWTR PAGHIGVAPN KGDTNVPTWP
     QDDEYAGRPQ KYYTKDVTGG WYDAGDHGKY VVNGGIAVWT LMNMYERAKI RGIANQGAYK
     DGGMNIPERN NGYPDILDEA RWEIEFFKKM QVTEKEDPSI AGMVHHKIHD FRWTALGMLP
     HEDPQPRYLR PVSTAATLNF AATLAQSARL WKDYDPTFAA DCLEKAEIAW QAALKHPDIY
     AEYTPGSGGP GGGPYNDDYV GDEFYWAACE LYVTTGKDEY KNYLMNSPHY LEMPAKMGEN
     GGANGEDNGL WGCFTWGTTQ GLGTITLALV ENGLPSADIQ KARNNIAKAA DKWLENIEEQ
     GYRLPIKQAE DERGGYPWGS NSFILNQMIV MGYAYDFTGN SKYLDGMQDG MSYLLGRNGL
     DQSYVTGYGE RPLQNPHDRF WTPQTSKKFP APPPGIIAGG PNSRFEDPTI TAAVKKDTPP
     QKCYIDHTDS WSTNEITINW NAPFAWVTAY LDEIDLITPP GGVDPEEPEV IYGDCNGDGK
     VNSTDAVALK RYILRSGISI NTDNADVNAD GRVNSTDLAI LKRYILKEID VLPHK
//