ID   E13B_ARTSW              Reviewed;         548 AA.
AC   Q59146;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   28-JUN-2023, entry version 89.
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;
GN   Name=glcI;
OS   Arthrobacter sp. (strain YCWD3).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=79671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Watanabe T., Hasegawa H., Tanaka H., Doi A., Doi K.;
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lysis of cellular walls containing beta-1,3-glucans.
CC       Implicated in the defense against fungal pathogens (By similarity).
CC       {ECO:0000250}.
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:0000250}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 64 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01350, ECO:0000305}.
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DR   EMBL; D23668; BAA04892.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59146; -.
DR   SMR; Q59146; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GH64; Glycoside Hydrolase Family 64.
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; cd09216; GH64-LPHase-like; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 3.30.920.50; Beta-1,3-glucanase, C-terminal domain; 1.
DR   Gene3D; 2.60.110.10; Thaumatin; 1.
DR   InterPro; IPR032477; Glyco_hydro_64.
DR   InterPro; IPR037398; Glyco_hydro_64_fam.
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; -; 1.
DR   PANTHER; PTHR38165:SF1; GLUCANASE B; 1.
DR   Pfam; PF16483; Glyco_hydro_64; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS52006; GH64; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Lectin;
KW   Periplasm; Signal.
FT   SIGNAL          1..36
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           37..548
FT                   /note="Glucan endo-1,3-beta-glucosidase"
FT                   /id="PRO_0000012234"
FT   DOMAIN          38..396
FT                   /note="GH64"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01350"
FT   DOMAIN          422..548
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   ACT_SITE        153
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01350"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01350"
SQ   SEQUENCE   548 AA;  58164 MW;  BD56354315750596 CRC64;
     MPHDRKNSSR RAWAALCAAV LAVSGALVGV AAPASAVPAT IPLTITNDSG RGPIYLYVLG
     ERDGVAGWAD AGGTFHPWPG GVGPVPVPAP DASIAGPGPG QSVTIRLPKL SGRVYYSYGQ
     KMTFQIVLDG RLVQPAVQND SDPNRNILFN WTEYTLNDGG LWINSTQVDH WSAPYQVGVQ
     RADGQVLSTG MLKPNGYEAF YTALESAGWG GLVQRAPDGS RLRALNPSHG IDVGKISSAS
     IDSYVTEVWN SYRTRDMCVT PFSHEPGTQF RGRVDGDWFR FRNGSGQEVA AFKKPDASSV
     YGCHKDLQAP NDHVVGPIAR TLCAALVRTT ALTNPNQPDA NSAGFYQDAR TNVYAKLAHQ
     QMANGKAYAF AFDDVGAHES LVHDGNPQAA YIKLDPFTGT ATPIANGGST EQPGTPGGLP
     AGTGALRIGS TLCLDVPWAD PTDTNQVQLA TCSGNAAQQW TRGTDGTVRA LGKCLDVARS
     GTADGTAVWI YTCNGTGAQK WTYDSATKAL RNPQSGKCLD AQGGAPLRDG QKVQLWTCNQ
     TEAQRWTL
//