ID   GUN2_THEFU     STANDARD;      PRT;   441 AA.
AC   P26222;
DT   01-MAY-1992 (Rel. 22, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Endoglucanase E-2 precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase E-2)
DE   (Cellulase E-2) (Cellulase E2).
GN   Name=celB;
OS   Thermomonospora fusca.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=2021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX;
RX   MEDLINE=91258320; PubMed=1904434;
RA   Lao G., Ghangas G.S., Jung E.D., Wilson D.B.;
RT   "DNA sequences of three beta-1,4-endoglucanase genes from
RT   Thermomonospora fusca.";
RL   J. Bacteriol. 173:3397-3407(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE, AND SEQUENCE REVISION.
RC   STRAIN=YX;
RA   Jung E.D., Lao G., Irwin D., Barr B., Benjamin A., Wilson D.B.;
RL   Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 32-47.
RA   Wilson D.B.;
RT   "Cellulases of Thermomonospora fusca.";
RL   Meth. Enzymol. 160:314-323(1988).
RN   [4]
RP   SUBUNIT, AND MUTAGENESIS OF GLU-163.
RX   PubMed=8347613;
RA   McGinnis K., Kroupis C., Wilson D.B.;
RT   "Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2.";
RL   Biochemistry 32:8146-8150(1993).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317.
RX   MEDLINE=94002001; PubMed=8399160;
RA   Spezio M., Wilson D.B., Karplus P.A.;
RT   "Crystal structure of the catalytic domain of a thermophilic
RT   endocellulase.";
RL   Biochemistry 32:9906-9916(1993).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- PATHWAY: Cellulose degradation.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B)
CC       family.
CC   -!- SIMILARITY: Contains 1 bacterial-type cellulose-binding (CBD)
CC       domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M73321; AAC06388.1; -.
DR   PIR; A42360; A42360.
DR   PIR; T12011; T12011.
DR   PDB; 1TML; X-ray; @=32-317.
DR   InterPro; IPR001919; Bac_celose-bind.
DR   InterPro; IPR008965; Cellul_bind.
DR   InterPro; IPR001524; Glyco_hydro_6.
DR   InterPro; IPR011253; Glyco_hydro_6-lk.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   ProDom; PD003733; Glyco_hydro_6; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   PROSITE; PS00561; CBD_BACTERIAL; 1.
DR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
KW   3D-structure; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     31
FT   CHAIN        32    441       Endoglucanase E-2.
FT   DOMAIN       32    320       Catalytic.
FT   DOMAIN      321    340       Linker.
FT   DOMAIN      341    441       Cellulose-binding.
FT   ACT_SITE    110    110
FT   ACT_SITE    148    148       Proton donor.
FT   ACT_SITE    296    296       Nucleophile.
FT   DISULFID    111    156
FT   DISULFID    263    298
FT   DISULFID    346    438       Potential.
FT   MUTAGEN     163    163       E->G: Loss of ability to form dimers.
FT   STRAND       36     36
FT   TURN         40     41
FT   HELIX        43     50
FT   TURN         52     53
FT   TURN         55     56
FT   HELIX        57     63
FT   TURN         64     66
FT   STRAND       69     69
FT   STRAND       71     73
FT   HELIX        78     95
FT   TURN         96     96
FT   STRAND       98     98
FT   STRAND      100    103
FT   TURN        109    112
FT   HELIX       122    134
FT   TURN        135    138
FT   STRAND      142    145
FT   TURN        147    148
FT   HELIX       149    153
FT   TURN        154    155
FT   HELIX       158    178
FT   TURN        180    181
FT   STRAND      183    187
FT   HELIX       196    205
FT   TURN        206    207
FT   HELIX       208    211
FT   STRAND      214    217
FT   TURN        219    220
FT   HELIX       225    239
FT   TURN        240    240
FT   TURN        242    243
FT   STRAND      245    249
FT   TURN        254    255
FT   TURN        259    260
FT   TURN        266    267
FT   STRAND      275    275
FT   TURN        281    282
FT   STRAND      283    288
FT   TURN        292    293
FT   STRAND      294    294
FT   TURN        302    303
FT   STRAND      305    305
FT   HELIX       307    315
FT   TURN        316    316
SQ   SEQUENCE   441 AA;  45844 MW;  87218E4537092AE5 CRC64;
     MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN NPNDPRTPVI
     RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI LVVYNAPGRD CGNHSSGGAP
     SHSAYRSWID EFAAGLKNRP AYIIVEPDLI SLMSSCMQHV QQEVLETMAY AGKALKAGSS
     QARIYFDAGH SAWHSPAQMA SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG
     NPSLRAVIDT SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA
     GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY TIANEWNDGF
     QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS SVTARNVGHN GTLSQGASTE
     FGFVGSKGNS NSVPTLTCAA S
//