ID   DEXT_STRSL              Reviewed;         822 AA.
AC   Q59979;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Dextranase;
DE            EC=3.2.1.11;
DE   AltName: Full=Alpha-1,6-glucan-6-glucanohydrolase;
DE   Flags: Precursor;
GN   Name=dex; Synonyms=dexS;
OS   Streptococcus salivarius.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M-33;
RX   PubMed=7737522; DOI=10.1016/0378-1119(95)00071-d;
RA   Ohnishi Y., Kubo S., Ono Y., Nozaki M., Gonda Y., Okano H., Matsuya T.,
RA   Matsushiro A., Morita T.;
RT   "Cloning and sequencing of the gene coding for dextranase from
RT   Streptococcus salivarius.";
RL   Gene 156:93-96(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in
CC         dextran.; EC=3.2.1.11;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 66 family. {ECO:0000305}.
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DR   EMBL; D29644; BAA06127.1; -; Genomic_DNA.
DR   PIR; JC4076; JC4076.
DR   AlphaFoldDB; Q59979; -.
DR   SMR; Q59979; -.
DR   CAZy; GH66; Glycoside Hydrolase Family 66.
DR   GO; GO:0033904; F:dextranase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14745; GH66; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR025092; Glyco_hydro_66.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF13199; Glyco_hydro_66; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..822
FT                   /note="Dextranase"
FT                   /id="PRO_0000012240"
FT   REGION          607..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..645
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  87924 MW;  31857D38D3F2C761 CRC64;
     MTVNLTLQHA SEIIGQDNVD LTLAAGASAK VSNLTVASEW LTNNTGYLVT ISVNDKSGNV
     LSSKRAGLSV EDDWTVFPRY GIVAGSPTDQ NSILVKNLEA YRKELELMKS MNINSYFFYD
     AYNEATDPFP EGVDSFVQKW NTWSHTQVDT KAVKELVDQV HKSGAVAMLY NMISADSNPK
     NPALPLAALA YNFYDSFGKK GEPMTYTIGD NPTQVYYDPA NPDWQKYIAG VMKSAMDRMG
     FDGWQGDTIG DNRVTDYEHR NSTDEADSHM MSDSYASFIN AMKDLIGEKY YITINDVNGG
     NDDKLAKARQ DVVYNELWTN GGSVIPGRMQ VAYGDLKARI DMVRNKTGKS LIVGAYMEEP
     GIDYTVPGGK ATNGAGKDAL AGKPLQADAT LLVDATVAAA GGYHMSIAAL ANANAALNVL
     QSAYYPTQYL SVAKDTIRKL YNYQQFITAY ENLLRGEGVT NSTQAVSTKN ASGEILSKDA
     LGVTGDQVWT FAKSGKGFST VQMINMMGIN AGWHNEEGYA DNKTPDAQEN LTVRLSLAGK
     TAQEAAKIAD QVYVTSPDDW ATSSMKKAQA SLETDENGQP VLVISVPKLT LWNMLYIKED
     TTATPVEPVT NQAGKKVDNT VTSEASSETA KSENTTVNKG SEAPTDTKPS VEAPKLDETT
     KPAPSVDELV NSAAVPVAIA VSETAHDKKD DNSVSNTDQG TVASDSITTP ASEAASTAAS
     TVSSEVSESV TVSSEPSETE NSSEASTSES ATPTTTAISE SHAVVEPVAS LTESESQAST
     SLVSETTSTI VSVAPSEVSE STSEEVILMD YQKTSIVGID SL