ID   GTF2_STRDO              Reviewed;        1592 AA.
AC   P27470;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 105.
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;
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=6715 / Serotype G;
RX   PubMed=1704006; DOI=10.1128/jb.173.3.989-996.1991;
RA   Abo H., Matsumura T., Kodama T., Ohta H., Fukui K., Kato K., Kagawa H.;
RT   "Peptide sequences for sucrose splitting and glucan binding within
RT   Streptococcus sobrinus glucosyltransferase (water-insoluble glucan
RT   synthetase).";
RL   J. Bacteriol. 173:989-996(1991).
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; D90213; BAA14241.1; -; Genomic_DNA.
DR   AlphaFoldDB; P27470; -.
DR   SMR; P27470; -.
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; 2.
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; 13.
PE   3: Inferred from homology;
KW   Dental caries; Glycosyltransferase; Repeat; Secreted; Signal; Transferase.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..1592
FT                   /note="Glucosyltransferase-I"
FT                   /id="PRO_0000021384"
FT   REPEAT          151..170
FT                   /note="Cell wall-binding 1"
FT   REPEAT          172..191
FT                   /note="Cell wall-binding 2"
FT   REPEAT          1083..1102
FT                   /note="Cell wall-binding 3"
FT   REPEAT          1103..1122
FT                   /note="Cell wall-binding 4"
FT   REPEAT          1167..1186
FT                   /note="Cell wall-binding 5"
FT   REPEAT          1211..1231
FT                   /note="Cell wall-binding 6"
FT   REPEAT          1232..1251
FT                   /note="Cell wall-binding 7"
FT   REPEAT          1276..1296
FT                   /note="Cell wall-binding 8"
FT   REPEAT          1297..1316
FT                   /note="Cell wall-binding 9"
FT   REPEAT          1411..1430
FT                   /note="Cell wall-binding 10"
FT   REPEAT          1455..1474
FT                   /note="Cell wall-binding 11"
FT   REPEAT          1523..1542
FT                   /note="Cell wall-binding 12"
FT   REPEAT          1567..1586
FT                   /note="Cell wall-binding 13"
FT   REGION          39..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..1044
FT                   /note="Catalytic; approximate"
FT   REGION          1093..1592
FT                   /note="Glucan-binding; approximate"
SQ   SEQUENCE   1592 AA;  176168 MW;  BC0A66D079351ECF CRC64;
     MEKNVRFKMH KVKKRWVTLS VASATMLASA LGASVASADT DTASDDSNQT VVTGDQTTNN
     QATDQTSIAA TATSEQSAST DAATDQASAA EQTQGTTAST DTAAQTTTNA NEAKWVPTEN
     ENQGFTDEML AEAKNVATAE SDSIPSDLAK MSNVKQVDGK YYYYDQDGNV KKNFAVSVGD
     KIYYFDETGA YKDTSKVDAD KSSSAVSQNA TIFAANNRAY STSAKNFEAV DNYLTADSWY
     RPKSILKDGK TWTESGKDDF RPLLMAWWPD TETKRNYVNY MNKVVGIDKT YTAETSQADL
     TAAAELVQAR IEQKITSENN TKWLREAISA FVKTQPQWNG ESEKPYDDHL QNGALLFDNQ
     TDLTPDTQSN YRLLNRTPTN QTGSLDSRFT YNPNDPLGGY DFLLANDVDN SNPVVQAEQL
     NWLHYLLNFG SIYANDADAN FDSIRVDAED NVDADQLQIS SDYLKAAYGI DKNNKNANNH
     VSIVEAWSDN DTPYLHDDGD NLMNMDNKFR LSMLWSLAKP TDVRSGLNPL IHNSLVDREV
     DDREVETVPS YSFARAHDSE VQDIIRDIIK AEINPNSFGY SFTQEEIDQA FKIYNEDLKK
     SDKKYTHYNV PLSYTLLLTN KGSIPRVYYG DMFTDDGQYM ANKTVNYDAI ESLLKARMKY
     VAGGQAMQNY QIGNGEILTS VRYGKGALKQ SDKGDATTRT SGVGVVMGNQ PNFSLDGKVV
     ALNMGAAHAN QEYRALMVST KDGVATYATD ADASKAGLVK RTDENGYLYF LNDDLKGVAN
     PQVSGFLQVW VPVGAADDQD IRVAASDTAS TDGKSLHQDA AMDSRVMFEG FSNFQSFATK
     EEEYTNVVIA NNVDKFVSWG ITDFEMAPQY VSSTDGQFQD SVIQNGYAFT DRYDLGMSKA
     NKYGTADQLV KAIKALHAKG LKVMADWVPD QMYTFPKQEV VTVTRTDKFG KPIAGSQINH
     SLYVTDTKSS GDDYQAKYGG AFLDELKEKY PELFTKKQMS TGQAIDPSVK IKQWSAKYFN
     GSNILGRGAD YVLSDQVSNK YFNVASDTLF LPSSLLGKVV ESGIRYDGKG YIYNSSATGD
     QVKASFITEA GNLYYFGKDG YMVTGAQTIN GANYFFLENG TALRNTIYTD AQGNSHYYAN
     DGKRYENENG YQQFGNDWRY FKDGNMAVGL TTVDGNVQYF DKDGVQAKDK IIVTRDGKVR
     YFDQHNGNAV TNTFIADKTG HWYYLGKDGV AVTGAQTVGK QKLYFEANGQ QVKGDFVTSD
     EGKLYFYDVD SGDMWTDTFI EDKAGNWFYL GKDGAAVTGA QTIRGQKLYF KANGQQVKGD
     IVKGTDGKIR YYDAKSGEQV FNKTVKAADG KTYVIGNDGV AVDPSVVKGQ TFKDASGALR
     FYNLKGQLVT GSGWYETANH DWVYIQSGKA LTGEQTINGQ HLYFKKDGHQ VKGQLVTGTD
     GKVRYYDANS GDQAFNKSVT VNGKTYYFGN DGTAQTAGNP KGQTFKDGSD IRFYSMEGQL
     VTGSGWYSNA QGQWLYVKNG KVLTGLQTVG SQRVYFDENG IQAKGKAVRT SDGKIRYFDE
     NSGSMITNQW KEVNGRYYYF GNDGARIYRG WN