ID   GTF1_STRDO              Reviewed;        1597 AA.
AC   P11001;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Glucosyltransferase-I;
DE            Short=GTF-I;
DE            EC=2.4.1.5;
DE   AltName: Full=Dextransucrase;
DE   AltName: Full=Sucrose 6-glucosyltransferase;
DE   Flags: Precursor;
GN   Name=gtfI;
OS   Streptococcus downei (Streptococcus sobrinus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MFE28;
RX   PubMed=3040686; DOI=10.1128/jb.169.9.4271-4278.1987;
RA   Ferretti J.J., Gilpin M.L., Russell R.R.B.;
RT   "Nucleotide sequence of a glucosyltransferase gene from Streptococcus
RT   sobrinus MFe28.";
RL   J. Bacteriol. 169:4271-4278(1987).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: GTF-I synthesizes water-insoluble glucans (alpha 1,3-
CC       linked glucose and some 1,6 linkages), GTF-S synthesizes water-soluble
CC       glucans (alpha 1,6-glucose). GTF-SI synthesizes both forms of glucans.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 70 family. {ECO:0000305}.
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DR   EMBL; M17391; AAC63063.1; -; Genomic_DNA.
DR   AlphaFoldDB; P11001; -.
DR   SMR; P11001; -.
DR   CAZy; GH70; Glycoside Hydrolase Family 70.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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   Pfam; PF01473; Choline_bind_1; 3.
DR   Pfam; PF19127; Choline_bind_3; 6.
DR   Pfam; PF02324; Glyco_hydro_70; 1.
DR   Pfam; PF19258; KxYKxGKxW_sig; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
DR   TIGRFAMs; TIGR04035; glucan_65_rpt; 5.
DR   TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR   PROSITE; PS51170; CW; 15.
PE   3: Inferred from homology;
KW   Dental caries; Glycosyltransferase; Repeat; Secreted; Signal; Transferase.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..1597
FT                   /note="Glucosyltransferase-I"
FT                   /id="PRO_0000021383"
FT   REPEAT          157..176
FT                   /note="Cell wall-binding 1"
FT   REPEAT          178..197
FT                   /note="Cell wall-binding 2"
FT   REPEAT          1089..1108
FT                   /note="Cell wall-binding 3"
FT   REPEAT          1109..1128
FT                   /note="Cell wall-binding 4"
FT   REPEAT          1130..1150
FT                   /note="Cell wall-binding 5"
FT   REPEAT          1152..1172
FT                   /note="Cell wall-binding 6"
FT   REPEAT          1173..1191
FT                   /note="Cell wall-binding 7"
FT   REPEAT          1193..1214
FT                   /note="Cell wall-binding 8"
FT   REPEAT          1216..1236
FT                   /note="Cell wall-binding 9"
FT   REPEAT          1237..1256
FT                   /note="Cell wall-binding 10"
FT   REPEAT          1258..1279
FT                   /note="Cell wall-binding 11"
FT   REPEAT          1281..1301
FT                   /note="Cell wall-binding 12"
FT   REPEAT          1302..1321
FT                   /note="Cell wall-binding 13"
FT   REPEAT          1323..1343
FT                   /note="Cell wall-binding 14"
FT   REPEAT          1344..1365
FT                   /note="Cell wall-binding 15"
FT   REPEAT          1366..1380
FT                   /note="Cell wall-binding 16"
FT   REPEAT          1415..1434
FT                   /note="Cell wall-binding 17"
FT   REPEAT          1436..1457
FT                   /note="Cell wall-binding 18"
FT   REPEAT          1459..1478
FT                   /note="Cell wall-binding 19"
FT   REPEAT          1485..1505
FT                   /note="Cell wall-binding 20"
FT   REPEAT          1508..1527
FT                   /note="Cell wall-binding 21"
FT   REPEAT          1528..1547
FT                   /note="Cell wall-binding 22"
FT   REPEAT          1549..1570
FT                   /note="Cell wall-binding 23"
FT   REPEAT          1572..1591
FT                   /note="Cell wall-binding 24"
FT   REGION          52..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..1050
FT                   /note="Catalytic; approximate"
FT   REGION          1099..1597
FT                   /note="Glucan-binding; approximate"
SQ   SEQUENCE   1597 AA;  177080 MW;  B9E86A200868798E CRC64;
     MEKNERFKMH KVKKRWVTIS VASATMLASA LGASVASADT ETVSEDSNQA VLTADQTTTN
     QDTEQTSVAA TATSEQSAST DAATDQASAT DQASAAEQTQ GTTASTDTAA QTTTNANEAK
     WVPTENENQV FTDEMLAEAK NVATAESNSI PSDLAKMSNV KQVDGKYYYY DQDGNVKKNF
     AVSVGEKIYY FDETGAYKDT SKVEADKSGS DISKEETTFA ANNRAYSTSA ENFEAIDNYL
     TADSWYRPKS ILKDGKTWTE SSKDDFRPLL MAWWPDTETK RNYVNYMNKV VGIDKTYTAE
     TSQADLTAAA ELVQARIEQK ITTEQNTKWL REAISAFVKT QPQWNGESEK PYDDHLQNGA
     LKFDNQSDLT PDTQSNYRLL NRTPTNQTGS LDSRFTYNAN DPLGGYELLL ANDVDNSNPI
     VQAEQLNWLH YLLNFGTIYA KDADANFDSI RVDAVDNVDA DLLQISSDYL KAAYGIDKNN
     KNANNHVSIV EAWSDNDTPY LHDDGDNLMN MDNKFRLSML WSLAKPLDKR SGLNPLIHNS
     LVDREVDDRE VETVPSYSFA RAHDSEVQDL IRDIIKAEIN PNAFGYSFTQ DEIDQAFKIY
     NEDLKKTDKK YTHYNVPLSY TLLLTNKGSI PRVYYGDMFT DDGQYMANKT VNYDAIESLL
     KARMKYVAGG QAMQNYQIGN GEILTSVRYG KGALKQSDKG DATTRTSGVG VVMGNQPNFS
     LDGKVVALNM GAAHANQEYR ALMVSTKDGV ATYATDADAS KAGLVKRTDE NGYLYFLNDD
     LKGVANPQVS GFLQVWVPVG AADDQDIRVA ASDTASTDGK SLHQDAAMDS RVMFEGFSNF
     QSFATKEEEY TNVVIANNVD KFVSWGITDF EMAPQYVSST DGQFLDSVIQ NGYAFTDRYD
     LGMSKANKYG TADQLVKAIK ALHAKGLKVM ADWVPDQMYT FPKQEVVTVT RTDKFGKPIA
     GSQINHSLYV TDTKSSGDDY QAKYGGAFLD ELKEKYPELF TKKQISTGQA IDPSVKIKQW
     SAKYFNGSNI LGRGADYVLS DQASNKYLNV SDDKLFLPKT LLGQVVESGI RFDGTGYVYN
     SSTTGEKVTD SFITEAGNLY YFGQDGYMVT GAQNIKGSNY YFLANGAALR NTVYTDAQGQ
     NHYYGNDGKR YENGYQQFGN DSWRYFKNGV MALGLTTVDG HVQYFDKDGV QAKDKIIVTR
     DGKVRYFDQH NGNAVTNTFV ADKTGHWYYL GKDGVAVTGA QTVGKQHLYF EANGQQVKGD
     FVTAKDGKLY FYDVDSGDMW TNTFIEDKAG NWFYLGKDGA AVTGAQTIKG QKLYFKANGQ
     QVKGDIVKDA DGKIRYYDAQ TGEQVFNKSV SVNGKTYYFG SDGTAQTQAN PKGQTFKDGS
     GVLRFYNLEG QYVSGSGWYE TAEHEWVYVK SGKVLTGAQT IGNQRVYFKD NGHQVKGQLV
     TGNDGKLRYY DANSGDQAFN KSVTVNGKTY YFGSDGTAQT QANPKGQTFK DGSGVLRFYN
     LEGQYVSGSG WYKNAQGQWL YVKDGKVLTG LQTVGNQKVY FDKNGIQAKG KAVRTSDGKV
     RYFDENSGSM ITNQWKFVYG QYYYFGSDGA AVYRGWN