CELK_ACET2
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 03-AUG-2022, entry version 88.
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; Firmicutes; 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 / 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 -!- 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 PRIDE; A3DCH1; -.
DR EnsemblBacteria; ABN51650; ABN51650; Cthe_0412.
DR KEGG; cth:Cthe_0412; -.
DR eggNOG; COG2273; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_006010_0_0_9; -.
DR OMA; GMNIPER; -.
DR OrthoDB; 1226595at2; -.
DR BioCyc; MetaCyc:MON-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; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 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 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; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR SUPFAM; SSF81296; SSF81296; 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
