ID   GTFS_STRDO              Reviewed;        1365 AA.
AC   P29336;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   13-SEP-2023, entry version 108.
DE   RecName: Full=Glucosyltransferase-S;
DE            Short=GTF-S;
DE            EC=2.4.1.5;
DE   AltName: Full=Dextransucrase;
DE   AltName: Full=Sucrose 6-glucosyltransferase;
DE   Flags: Precursor;
GN   Name=gtfS;
OS   Streptococcus downei (Streptococcus sobrinus).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MFE28;
RX   PubMed=2142479; DOI=10.1128/iai.58.8.2452-2458.1990;
RA   Gilmore K.S., Russell R.R., Ferretti J.J.;
RT   "Analysis of the Streptococcus downei gtfS gene, which specifies a
RT   glucosyltransferase that synthesizes soluble glucans.";
RL   Infect. Immun. 58:2452-2458(1990).
CC   -!- FUNCTION: Production of extracellular glucans, that are thought to play
CC       a key role in the development of the dental plaque because of their
CC       ability to adhere to smooth surfaces and mediate the aggregation of
CC       bacterial cells and food debris.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->6)-alpha-D-glucosyl](n) + sucrose = [(1->6)-alpha-D-
CC         glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:18825, Rhea:RHEA-
CC         COMP:11144, Rhea:RHEA-COMP:11145, ChEBI:CHEBI:17992,
CC         ChEBI:CHEBI:18269, ChEBI:CHEBI:37721; EC=2.4.1.5;
CC   -!- ACTIVITY REGULATION: Glucan synthesis by GTF-S is independent of primer
CC       glucan unlike GTF-I.
CC   -!- MISCELLANEOUS: Synthesizes water-soluble glucans (alpha 1,6-glucose).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 70 family. {ECO:0000305}.
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DR   EMBL; M30943; AAA26898.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29336; -.
DR   SMR; P29336; -.
DR   CAZy; GH70; Glycoside Hydrolase Family 70.
DR   GO; GO:0047849; F:dextransucrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046527; F:glucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009250; P:glucan biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1.
DR   Gene3D; 2.10.270.10; Cholin Binding; 4.
DR   Gene3D; 3.20.20.470; Glucansucrase; 1.
DR   Gene3D; 2.30.30.420; glucansucrase; 1.
DR   InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR   InterPro; IPR027636; Glucan-bd_rpt.
DR   InterPro; IPR003318; Glyco_hydro70cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR022263; KxYKxGKxW.
DR   NCBIfam; TIGR04035; glucan_65_rpt; 4.
DR   NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR   Pfam; PF01473; Choline_bind_1; 1.
DR   Pfam; PF19127; Choline_bind_3; 5.
DR   Pfam; PF02324; Glyco_hydro_70; 1.
DR   Pfam; PF19258; KxYKxGKxW_sig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF69360; Cell wall binding repeat; 3.
DR   PROSITE; PS51170; CW; 12.
PE   3: Inferred from homology;
KW   Dental caries; Glycosyltransferase; Repeat; Signal; Transferase.
FT   SIGNAL          1..36
FT                   /note="Or 37"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..1365
FT                   /note="Glucosyltransferase-S"
FT                   /id="PRO_0000021388"
FT   REPEAT          146..166
FT                   /note="Cell wall-binding 1"
FT   REPEAT          168..187
FT                   /note="Cell wall-binding 2"
FT   REPEAT          1052..1071
FT                   /note="Cell wall-binding 3"
FT   REPEAT          1073..1092
FT                   /note="Cell wall-binding 4"
FT   REPEAT          1093..1112
FT                   /note="Cell wall-binding 5"
FT   REPEAT          1113..1133
FT                   /note="Cell wall-binding 6"
FT   REPEAT          1136..1159
FT                   /note="Cell wall-binding 7"
FT   REPEAT          1160..1179
FT                   /note="Cell wall-binding 8"
FT   REPEAT          1234..1253
FT                   /note="Cell wall-binding 9"
FT   REPEAT          1278..1298
FT                   /note="Cell wall-binding 10"
FT   REPEAT          1299..1318
FT                   /note="Cell wall-binding 11"
FT   REPEAT          1343..1362
FT                   /note="Cell wall-binding 12"
FT   REGION          80..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..1000
FT                   /note="Catalytic; approximate"
FT   COMPBIAS        127..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1365 AA;  151591 MW;  167296B5A2E8C476 CRC64;
     MEKNLRYKLH KVKKQWVAIG VTTVTLSFLA GGQVVAADTN NNDGTSVQVN KMVPSDPKFD
     AQAQNGQLAQ AMFKAANQAD QTATSQVSPA TDGRVDNQVT PAANQPAANV ANQDVANPAT
     DAGALNRQSA ADTSTDGKAV PQTSDQPGHL ETVDGKTYYV DANGQRLKNY SMVIDGKTYY
     FDGQTGEAQT DLPKTGQANQ DNVPDSYQAN NQAYSNEASS FETVDNYLTA DSWYRPRKIL
     KNGQSWQASS EGDLRPILMT WWPDAATKAA YANFWAKEGL ISGSYRQNSA NLDAATQNIQ
     SAIEKKIASE GNTNWLRDKM SQFVKSQNQW SIASENETVY PNQDHMQGGA LLFSNSKDTE
     HANSDWRLLN RNPTFQTGKQ KYFTTNYAGY ELLLANDVDN SNPVVQAEQL NHLHYLMNWG
     DIVMGDKDAN FDGVRVDAVD NVNADLLQIQ RDYYKAKYGT DQNEKNAIDH LSILEAWSGN
     DNDYVKDQNN FSLSIDNDQR SGMLKAFGYA SAYRGNLSNL ATAGLKNRSA NPDSDPVPNY
     VFIRAHDSEV QTRIAKIIRE KLGKTNADGL TNLTLDDLNK AFDIYNQDMN ATDKVYYPNN
     LPMAYAWMLQ NKDTVTRVYY GDMYTDNGQY MATKTPFYNA IETLLKGRIK YVAGGQAVSY
     KQDWSSGILT SVRYGKGANS ASDAGNTETR NSGMALLINN RPNFRAYRNL TLNMGAAHKS
     QAYRPLLLST KDGIATYLND SDVDSRQYKY TDSQGNLSFS ASELQSVANA QVSGMIQVWV
     PVGAADNQDV RTSPSTQATK DGNIYHQSDA LDSQVIYEGF SNFQAFAQSP DQYTNAVIAK
     NGDLFKSWGI TQFEMAPQYV SSEDGTFLDS VILNGYAFSD RYDLAMSKNN KYGSKQDLAN
     AIKGLQSAGI KVLSDLVPNQ LYNLPGKEVV TATRVNQYGQ AKSGATINKT PYVANTRSYG
     DYQEQYGGKF LDDLQKLYPR LFSTKQISTG KPIDPSVKIT NWSAKYFNGS NILGRGAKYV
     LSEGNKYLNL ADGKLFLPTV LNNTYGQPQV SANGFISKNG GIHYLDKNGQ EVKNRFKEIS
     GSWYYFDSDG KMATGKTKIG NDTYLFMPNG KQLKEGVWYD GKKAYYYDDN GRTWTNKGFV
     EFRVDGQDKW RYFNGDGTIA IGLVSLDNRT LYFDAYGYQV KGQTVTINGK SYTFDADQGD
     LVQTDNANPA PQGQAGWKLL GDNQWGYRKD GQLLTGEQTI DGQKVFFQDN GVQVKGGTAT
     DASGVLRFYD RDQGHQVGKG WYSTSDDNWV YVNESGQVLT GLQTIDGQTV YFDDKGIQAK
     GKAVWDENGN LRYFDADSGN MLRDRWKNVD GNWYYFNRNG LATRW
//