ID   GUB_ACET2               Reviewed;         334 AA.
AC   A3DBX3; P29716; P37074;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Beta-glucanase;
DE            EC=3.2.1.73;
DE   AltName: Full=1,3-1,4-beta-D-glucan 4-glucanohydrolase;
DE   AltName: Full=Endo-beta-1,3-1,4 glucanase;
DE   AltName: Full=Laminarinase;
DE   AltName: Full=Lichenase;
DE   Flags: Precursor;
GN   Name=licB; Synonyms=lam1; OrderedLocusNames=Cthe_0211;
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 [GENOMIC DNA].
RX   PubMed=1740123; DOI=10.1111/j.1432-1033.1992.tb16600.x;
RA   Schimming S., Schwarz W.H., Staudenbauer W.L.;
RT   "Structure of the Clostridium thermocellum gene licB and the encoded beta-
RT   1,3-1,4-glucanase. A catalytic region homologous to Bacillus lichenases
RT   joined to the reiterated domain of clostridial cellulases.";
RL   Eur. J. Biochem. 204:13-19(1992).
RN   [2]
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 beta-D-
CC         glucans containing (1->3)- and (1->4)-bonds.; EC=3.2.1.73;
CC   -!- SUBUNIT: May form part of a multienzyme complex (cellulosome).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; X63355; CAA44959.1; -; Genomic_DNA.
DR   EMBL; CP000568; ABN51452.1; -; Genomic_DNA.
DR   PIR; S23498; S23498.
DR   RefSeq; WP_003512300.1; NC_009012.1.
DR   PDB; 3WVJ; X-ray; 1.95 A; A/B=30-249.
DR   PDBsum; 3WVJ; -.
DR   AlphaFoldDB; A3DBX3; -.
DR   SMR; A3DBX3; -.
DR   STRING; 203119.Cthe_0211; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GeneID; 57419464; -.
DR   KEGG; cth:Cthe_0211; -.
DR   eggNOG; COG2273; Bacteria.
DR   HOGENOM; CLU_071026_1_0_9; -.
DR   OrthoDB; 9809583at2; -.
DR   BioCyc; MetaCyc:MONOMER-16465; -.
DR   BRENDA; 3.2.1.73; 1530.
DR   Proteomes; UP000002145; Chromosome.
DR   GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd14256; Dockerin_I; 1.
DR   CDD; cd02175; GH16_lichenase; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR008264; Beta_glucanase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF185; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 6-RELATED; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PRINTS; PR00737; GLHYDRLASE16.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..334
FT                   /note="Beta-glucanase"
FT                   /id="PRO_0000284719"
FT   DOMAIN          28..248
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   DOMAIN          267..334
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   ACT_SITE        136
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        140
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          84..92
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          103..111
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          118..126
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          163..166
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          176..183
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          186..191
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          208..219
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   HELIX           221..224
FT                   /evidence="ECO:0007829|PDB:3WVJ"
FT   STRAND          233..245
FT                   /evidence="ECO:0007829|PDB:3WVJ"
SQ   SEQUENCE   334 AA;  37897 MW;  0837564E9726F281 CRC64;
     MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE KADWANGSVF
     NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRTKSF FGYGYYEVRM KAAKNVGIVS
     SFFTYTGPSD NNPWDEIDIE FLGKDTTKVQ FNWYKNGVGG NEYLHNLGFD ASQDFHTYGF
     EWRPDYIDFY VDGKKVYRGT RNIPVTPGKI MMNLWPGIGV DEWLGRYDGR TPLQAEYEYV
     KYYPNGVPQD NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP
     VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL
//