CELK_ACETH
ID CELK_ACETH Reviewed; 895 AA.
AC P0C2S1; O68438; Q10748; Q4CGG7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Cellulose 1,4-beta-cellobiosidase;
DE EC=3.2.1.91;
DE Flags: Precursor;
GN Name=celK;
OS Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1515;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 283-287 AND 326-337,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=JW20;
RX PubMed=10464199; DOI=10.1128/jb.181.17.5288-5295.1999;
RA Kataeva I., Li X.L., Chen H., Choi S.-K., Ljungdahl L.G.;
RT "Cloning and sequence analysis of a new cellulase gene encoding CelK, a
RT major cellulosome component of Clostridium thermocellum: evidence for gene
RT duplication and recombination.";
RL J. Bacteriol. 181:5288-5295(1999).
RN [2]
RP PROTEIN SEQUENCE OF 28-45, AND SUBCELLULAR LOCATION.
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).
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; Evidence={ECO:0000269|PubMed:10464199};
CC -!- ACTIVITY REGULATION: Inhibited by cellobiose.
CC {ECO:0000269|PubMed:10464199}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.67 uM for PNP-cellobioside {ECO:0000269|PubMed:10464199};
CC Vmax=15.1 umol/min/mg enzyme {ECO:0000269|PubMed:10464199};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:10464199};
CC Temperature dependence:
CC Retains 97% of original activity when incubated for 200 hours at 60
CC degrees Celsius. {ECO:0000269|PubMed:10464199};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10464199,
CC ECO:0000269|PubMed:8664281}.
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; AF039030; AAC06139.1; -; Genomic_DNA.
DR PDB; 3P6B; X-ray; 2.00 A; A/B=27-210.
DR PDBsum; 3P6B; -.
DR AlphaFoldDB; P0C2S1; -.
DR SMR; P0C2S1; -.
DR CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR SABIO-RK; P0C2S1; -.
DR EvolutionaryTrace; P0C2S1; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:8664281"
FT CHAIN 28..895
FT /note="Cellulose 1,4-beta-cellobiosidase"
FT /id="PRO_0000045748"
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 REGION 241..815
FT /note="Catalytic"
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"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3P6B"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:3P6B"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:3P6B"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3P6B"
FT STRAND 184..197
FT /evidence="ECO:0007829|PDB:3P6B"
SQ SEQUENCE 895 AA; 100712 MW; 5DB1FD84A6750CCE CRC64;
MNFRRMLCAA IVLTIVLSIM LPSTVFALED KSSKLPDYKN 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 PAGHIGIEPN 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 ENGLPATDIQ KARNNIAKAA DRWLENIEEQ
GYRLPIKQAE DERGGYPWGS NSFILNQMIV MGYAYDFTGN SKYLDGMQDG MSYLLGRNGL
DQSYVTGYGE RPLQNPHDRF WTPQTSKKFP APPPGIIAGG PNSRFEDPTI TAAVKKDTPP
QKCYIDHTDS WSTNEITVNW NAPFAWVTAY LDEIDLITPP GGVDPEEPEV IYGDCNGDGK
VNSTDAVALK RYILRSGISI NTDNADVNAD GRVNSTDLAI LKRYILKEID VLPHK
