ID   E13B_CELCE              Reviewed;         548 AA.
AC   P22222;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase;
DE            Short=(1->3)-beta-glucanase;
DE   Flags: Precursor;
OS   Cellulosimicrobium cellulans (Arthrobacter luteus).
OC   Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae;
OC   Cellulosimicrobium.
OX   NCBI_TaxID=1710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-63, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=1985933; DOI=10.1016/s0021-9258(17)35282-1;
RA   Shen S.-H., Chretien P., Bastien L., Slilaty S.N.;
RT   "Primary sequence of the glucanase gene from Oerskovia xanthineolytica.
RT   Expression and purification of the enzyme from Escherichia coli.";
RL   J. Biol. Chem. 266:1058-1063(1991).
CC   -!- FUNCTION: Lysis of cellular walls containing beta-1,3-glucans.
CC       Implicated in the defense against fungal pathogens.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1985933}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 64 family. {ECO:0000305}.
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DR   EMBL; M60826; AAA25520.1; -; Genomic_DNA.
DR   PIR; A39094; A39094.
DR   AlphaFoldDB; P22222; -.
DR   SMR; P22222; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GH64; Glycoside Hydrolase Family 64.
DR   PRIDE; P22222; -.
DR   BRENDA; 3.2.1.39; 447.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.60.110.10; -; 1.
DR   Gene3D; 3.30.920.50; -; 1.
DR   InterPro; IPR037398; Glyco_hydro_64.
DR   InterPro; IPR032477; Glyco_hydro_64_N.
DR   InterPro; IPR042517; Glyco_hydro_64_N_2.
DR   InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR38165; PTHR38165; 1.
DR   Pfam; PF16483; Glyco_hydro_64; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; SSF50370; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Lectin; Periplasm; Signal.
FT   SIGNAL          1..36
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:1985933"
FT   CHAIN           37..548
FT                   /note="Glucan endo-1,3-beta-glucosidase"
FT                   /id="PRO_0000012235"
FT   DOMAIN          422..548
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          37..430
FT                   /note="Possesses beta-glucanase activity, but is unable to
FT                   lyse viable cells"
FT   REGION          472..548
FT                   /note="Essential for the lytic activity, but not for the
FT                   beta-glucanase function"
SQ   SEQUENCE   548 AA;  58089 MW;  412B5A4AA24C048D CRC64;
     MPHDRKNSSR RAWAALCAAV LAVSGALVGV AAPASAVPAT IPLTITNDSG RGPIYLYVLG
     ERDGVAGWAD AGGTFHPWPG GVGPVPVPAP DASIAGPGPG QSVTIRLPKL SGRVYYSYGQ
     KMTFQIVLDG RLVQPAVQND SDPNRNILFN WTEYTLNDGG LWINSTQVDH WSAPYQVGVQ
     RADGQVLSTG MLKPNGYEAF YTALEGAGWG GLVQRAPDGS RLRALNPSHG IDVGKISSAS
     IDSYVTEVWN SYRTRDMVVT PFSHEPGTQF RGRVDGDWFR FRSGSGQEVA AFKKPDASSV
     YGCHKDLQAP NDHVVGPIAR TLCAALVRTT ALTNPNQPDA NSAGFYQDAR TNVYAKLAHQ
     QMANGKAYAF AFDDVGAHES LVHDGNPQAA YIKLDPFTGT ATPLGNGGST EQPGTPGGLP
     AGTGALRIGS TLCLDVPWAD PTDTNQVQLA TCSGNAAQQW TRGTDGTVRA LGKCLDVARS
     GTADGTAVWI YTCNGTGAQK WTYDSATKAL RNPQSGKCLD AQGGAPLRDG QKVQLWTCNQ
     TEAQRWTL