ID   E13B_NIACI              Reviewed;         682 AA.
AC   P23903;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-MAY-2023, entry version 90.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase A1;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase;
DE   AltName: Full=(1->3)-beta-glucanase A1;
DE   Flags: Precursor;
GN   Name=glcA;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 39-52.
RC   STRAIN=WL-12;
RX   PubMed=2311931; DOI=10.1016/0378-1119(90)90122-8;
RA   Yahata N., Watanabe T., Nakamura Y., Yamamoto Y., Kamimiya S., Tanaka H.;
RT   "Structure of the gene encoding beta-1,3-glucanase A1 of Bacillus circulans
RT   WL-12.";
RL   Gene 86:113-117(1990).
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: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; M34503; AAA22474.1; -; Genomic_DNA.
DR   PIR; JQ0420; JQ0420.
DR   AlphaFoldDB; P23903; -.
DR   SMR; P23903; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   CDD; cd08023; GH16_laminarinase_like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000269|PubMed:2311931"
FT   CHAIN           39..682
FT                   /note="Glucan endo-1,3-beta-glucosidase A1"
FT                   /id="PRO_0000011796"
FT   DOMAIN          391..682
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        552
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        557
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
SQ   SEQUENCE   682 AA;  75466 MW;  8C4F407E34D4ADD5 CRC64;
     MKPSHFTEKR FMKKVLGLFL VVVMLASVGV LPTSKVQAAG TTVTSMEYFS PADGPVISKS
     GVGKASYGFV MPKFNGGSAT WNDVYSDVGV NVKVGNNWVD IDQAGGYIYN QNWGHWSDGG
     FNGYWFTLSA TTEIQLYSKA NGVKLEYQLV FQNINKTTIT AMNPTQGPQI TASFTGGAGF
     TYPTFNNDSA VTYEAVADDL KVYVKPVNSS SWIDIDNNAA SGWIYDHNFG QFTDGGGGYW
     FNVTESINVK LESKTSSANL VYTITFNEPT RNSYVITPYE GTTFTADANG SIGIPLPKID
     GGAPIAKELG NFVYQINING QWVDLSNSSQ SKFAYSANGY NNMSDANQWG YWADYIYGLW
     FQPIQENMQI RIGYPLNGQA GGNIGNNFVN YTFIGNPNAP RPDVSDQEDI SIGTPTDPAI
     AGMNLIWQDE FNGTTLDTSK WNYETGYYLN NDPATWGWGN AELQHYTNST QNVYVQDGKL
     NIKAMNDSKS FPQDPNRYAQ YSSGKINTKD KLSLKYGRVD FRAKLPTGDG VWPALWMLPK
     DSVYGTWAAS GEIDVMEARG RLPGSVSGTI HFGGQWPVNQ SSGGDYHFPE GQTFANDYHV
     YSVVWEEDNI KWYVDGKFFY KVTNQQWYST AAPNNPNAPF DEPFYLIMNL AVGGNFDGGR
     TPNASDIPAT MQVDYVRVYK EQ
//