ID   GUN_ALKA3               Reviewed;         800 AA.
AC   P06564;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Alkaline cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
OS   Alkalihalobacillus akibai (strain ATCC 43226 / DSM 21942 / CIP 109018 / JCM
OS   9157 / 1139) (Bacillus akibai).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=1236973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3098909; DOI=10.1099/00221287-132-8-2329;
RA   Fukumori F., Kudo T., Narahashi Y., Horikoshi K.;
RT   "Molecular cloning and nucleotide sequence of the alkaline cellulase gene
RT   from the alkalophilic Bacillus sp. strain 1139.";
RL   J. Gen. Microbiol. 132:2329-2335(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.0.;
CC   -!- MISCELLANEOUS: Alkalophilic Bacillus sp strain 1139 is not a true
CC       cellulolytic microorganism because the enzyme is unable to hydrolyze
CC       native cellulose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; M15743; AAA22305.1; -; Genomic_DNA.
DR   EMBL; D00066; BAA00045.1; -; Genomic_DNA.
DR   PIR; A29003; A29003.
DR   PDB; 1UWW; X-ray; 1.40 A; A/B=571-761.
DR   PDBsum; 1UWW; -.
DR   AlphaFoldDB; P06564; -.
DR   SMR; P06564; -.
DR   STRING; 1236973.JCM9157_4362; -.
DR   CAZy; CBM17; Carbohydrate-Binding Module Family 17.
DR   CAZy; CBM28; Carbohydrate-Binding Module Family 28.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   eggNOG; COG2730; Bacteria.
DR   EvolutionaryTrace; P06564; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005086; CBM_fam_17/28.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF03424; CBM_17_28; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..800
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000007837"
FT   REGION          761..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..800
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        305
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   STRAND          588..590
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          594..596
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          600..602
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          613..617
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          620..628
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   TURN            637..640
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          643..647
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          658..669
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          674..681
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   HELIX           684..686
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          696..699
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   HELIX           700..705
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          712..720
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          735..744
FT                   /evidence="ECO:0007829|PDB:1UWW"
FT   STRAND          748..759
FT                   /evidence="ECO:0007829|PDB:1UWW"
SQ   SEQUENCE   800 AA;  88602 MW;  7CCA4D7B6DAD55CF CRC64;
     MMLRKKTKQL ISSILILVLL LSLFPTALAA EGNTREDNFK HLLGNDNVKR PSEAGALQLQ
     EVDGQMTLVD QHGEKIQLRG MSTHGLQWFP EILNDNAYKA LANDWESNMI RLAMYVGENG
     YASNPELIKS RVIKGIDLAI ENDMYVIVDW HVHAPGDPRD PVYAGAEDFF RDIAALYPNN
     PHIIYELANE PSSNNNGGAG IPNNEEGWNA VKEYADPIVE MLRDSGNADD NIIIVGSPNW
     SQRPDLAADN PIDDHHTMYT VHFYTGSHAA STESYPPETP NSERGNVMSN TRYALENGVA
     VFATEWGTSQ ANGDGGPYFD EADVWIEFLN ENNISWANWS LTNKNEVSGA FTPFELGKSN
     ATSLDPGPDQ VWVPEELSLS GEYVRARIKG VNYEPIDRTK YTKVLWDFND GTKQGFGVNG
     DSPVEDVVIE NEAGALKLSG LDASNDVSEG NYWANARLSA DGWGKSVDIL GAEKLTMDVI
     VDEPTTVSIA AIPQGPSANW VNPNRAIKVE PTNFVPLEDK FKAELTITSA DSPSLEAIAM
     HAENNNINNI ILFVGTEGAD VIYLDNIKVI GTEVEIPVVH DPKGEAVLPS VFEDGTRQGW
     DWAGESGVKT ALTIEEANGS NALSWEFGYP EVKPSDNWAT APRLDFWKSD LVRGENDYVT
     FDFYLDPVRA TEGAMNINLV FQPPTNGYWV QAPKTYTINF DELEEPNQVN GLYHYEVKIN
     VRDITNIQDD TLLRNMMIIF ADVESDFAGR VFVDNVRFEG AATTEPVEPE PVDPGEETPP
     VDEKEAKTEQ KEAEKEEKEE