ID GTFB_STRMU Reviewed; 1476 AA. AC P08987; O69381; O69384; O69387; O69390; O69396; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 3. DT 27-MAR-2024, entry version 173. 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=gtfB; OrderedLocusNames=SMU_1004; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=GS-5; RX PubMed=3040685; DOI=10.1128/jb.169.9.4263-4270.1987; RA Shiroza T., Ueda S., Kuramitsu H.K.; RT "Sequence analysis of the gtfB gene from Streptococcus mutans."; RL J. Bacteriol. 169:4263-4270(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MT4239 / Serotype c, MT4245 / Serotype e, MT4251 / Serotype f, RC MT4467 / Serotype e, and MT8148 / Serotype c; RX PubMed=9570124; DOI=10.1111/j.1574-6968.1998.tb12965.x; RA Fujiwara T., Terao Y., Hoshino T., Kawabata S., Ooshima T., Sobue S., RA Kimura S., Hamada S.; RT "Molecular analyses of glucosyltransferase genes among strains of RT Streptococcus mutans."; RL FEMS Microbiol. Lett. 161:331-336(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M17361; AAA88588.1; -; Genomic_DNA. DR EMBL; D88651; BAA26101.1; -; Genomic_DNA. DR EMBL; D88654; BAA26105.1; -; Genomic_DNA. DR EMBL; D88657; BAA26109.1; -; Genomic_DNA. DR EMBL; D88660; BAA26113.1; -; Genomic_DNA. DR EMBL; D89977; BAA26119.1; -; Genomic_DNA. DR EMBL; AE014133; AAN58705.1; -; Genomic_DNA. DR PIR; B33135; B33135. DR RefSeq; NP_721399.1; NC_004350.2. DR RefSeq; WP_002352268.1; NC_004350.2. DR PDB; 8FG8; X-ray; 2.35 A; A/B=191-1051. DR PDB; 8FJ9; X-ray; 2.50 A; A/B=191-1051. DR PDB; 8FJC; X-ray; 2.50 A; A/B=191-1051. DR PDB; 8FK4; X-ray; 3.25 A; A/B/C/D/E/F/G/H=191-1051. DR PDB; 8FKL; X-ray; 1.48 A; A=421-940. DR PDB; 8UF5; X-ray; 2.50 A; A/B=191-1051. DR PDBsum; 8FG8; -. DR PDBsum; 8FJ9; -. DR PDBsum; 8FJC; -. DR PDBsum; 8FK4; -. DR PDBsum; 8FKL; -. DR PDBsum; 8UF5; -. DR AlphaFoldDB; P08987; -. DR SMR; P08987; -. DR STRING; 210007.SMU_1004; -. DR ChEMBL; CHEMBL3822351; -. DR CAZy; GH70; Glycoside Hydrolase Family 70. DR ABCD; P08987; 3 sequenced antibodies. DR KEGG; smu:SMU_1004; -. DR PATRIC; fig|210007.7.peg.897; -. DR eggNOG; COG0366; Bacteria. DR eggNOG; COG5263; Bacteria. DR HOGENOM; CLU_001623_1_0_9; -. DR OrthoDB; 2032428at2; -. DR PhylomeDB; P08987; -. DR SABIO-RK; P08987; -. DR PHI-base; PHI:7053; -. DR Proteomes; UP000002512; Chromosome. 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 Gene3D; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1. DR Gene3D; 2.10.270.10; Cholin Binding; 3. 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; 6. DR NCBIfam; TIGR03715; KxYKxGKxW; 1. DR Pfam; PF01473; Choline_bind_1; 1. DR Pfam; PF19127; Choline_bind_3; 6. 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; 13. PE 1: Evidence at protein level; KW 3D-structure; Dental caries; Glycosyltransferase; Reference proteome; KW Repeat; Secreted; Signal; Transferase. FT SIGNAL 1..34 FT /evidence="ECO:0000255" FT CHAIN 35..1476 FT /note="Glucosyltransferase-I" FT /id="PRO_0000021385" FT REPEAT 159..178 FT /note="Cell wall-binding 1" FT REPEAT 179..199 FT /note="Cell wall-binding 2" FT REPEAT 1087..1106 FT /note="Cell wall-binding 3" FT REPEAT 1107..1126 FT /note="Cell wall-binding 4" FT REPEAT 1170..1189 FT /note="Cell wall-binding 5" FT REPEAT 1214..1234 FT /note="Cell wall-binding 6" FT REPEAT 1235..1254 FT /note="Cell wall-binding 7" FT REPEAT 1279..1299 FT /note="Cell wall-binding 8" FT REPEAT 1300..1319 FT /note="Cell wall-binding 9" FT REPEAT 1344..1364 FT /note="Cell wall-binding 10" FT REPEAT 1365..1384 FT /note="Cell wall-binding 11" FT REPEAT 1409..1429 FT /note="Cell wall-binding 12" FT REPEAT 1430..1449 FT /note="Cell wall-binding 13" FT REGION 42..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 102..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..1051 FT /note="Catalytic; approximate" FT VARIANT 62 FT /note="S -> T (in strain: MT4239)" FT VARIANT 65 FT /note="T -> I (in strain: GS-5)" FT VARIANT 68 FT /note="V -> A (in strain: GS-5, MT4245, MT4251, MT4467 and FT MT8148)" FT VARIANT 78 FT /note="Q -> P (in strain: MT4251)" FT VARIANT 86 FT /note="I -> S (in strain: GS-5, MT4245, MT4251, MT4467 and FT MT8148)" FT VARIANT 89 FT /note="S -> F (in strain: MT4251)" FT VARIANT 168 FT /note="K -> N (in strain: MT4251)" FT VARIANT 276 FT /note="S -> D (in strain: GS-5, MT4467 and MT8148)" FT VARIANT 399 FT /note="N -> R (in strain: MT4239)" FT VARIANT 474 FT /note="I -> T (in strain: MT4239)" FT VARIANT 512 FT /note="K -> R (in strain: MT8148)" FT VARIANT 519 FT /note="F -> Y (in strain: MT8148)" FT VARIANT 701 FT /note="T -> I (in strain: MT8148)" FT VARIANT 708 FT /note="A -> V (in strain: MT8148)" FT VARIANT 938 FT /note="F -> L (in strain: MT8148)" FT VARIANT 952..957 FT /note="FGKPVE -> YGTPVA (in strain: GS-5, MT4239 and FT MT4467)" FT VARIANT 963..964 FT /note="SV -> NT (in strain: GS-5, MT4239 and MT4467)" FT VARIANT 968..970 FT /note="ADS -> VDG (in strain: GS-5, MT4239 and MT4467)" FT VARIANT 1086 FT /note="A -> T (in strain: MT4239)" FT VARIANT 1158 FT /note="S -> N (in strain: MT4239)" FT VARIANT 1163 FT /note="H -> Y (in strain: MT4251)" FT VARIANT 1168 FT /note="E -> K (in strain: MT8148)" FT VARIANT 1182 FT /note="Y -> C (in strain: MT8148)" FT VARIANT 1234 FT /note="A -> P (in strain: MT4239)" FT VARIANT 1263 FT /note="R -> H (in strain: GS-5 and MT4467)" FT VARIANT 1263 FT /note="R -> P (in strain: MT8148)" FT VARIANT 1264 FT /note="Y -> H (in strain: GS-5, MT4239, MT4467 and MT8148)" FT VARIANT 1272 FT /note="S -> G (in strain: GS-5, MT4239, MT4467 and MT8148)" FT VARIANT 1329 FT /note="H -> Y (in strain: GS-5 and MT4467)" FT VARIANT 1394 FT /note="Y -> H (in strain: GS-5, MT4239, MT4467 and MT8148)" FT VARIANT 1402 FT /note="S -> G (in strain: GS-5, MT4239, MT4467 and MT8148)" FT VARIANT 1459 FT /note="Y -> H (in strain: MT4467)" FT CONFLICT 570 FT /note="R -> A (in Ref. 1; AAA88588)" FT /evidence="ECO:0000305" FT CONFLICT 800..817 FT /note="ADQDVRVAASTAPSTDGK -> LIKMFALRLARPHQQMA (in Ref. 1; FT AAA88588)" FT /evidence="ECO:0000305" FT CONFLICT 1310 FT /note="H -> L (in Ref. 1; AAA88588)" FT /evidence="ECO:0000305" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 220..222 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 248..253 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 257..260 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 277..291 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 303..324 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 328..338 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 384..388 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 408..412 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 417..431 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 433..438 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 447..450 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 453..455 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 459..472 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 474..476 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 478..482 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 495..502 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 504..509 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 511..521 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 533..536 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 537..540 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 543..545 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 554..556 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 563..565 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 566..576 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 588..603 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 608..610 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 614..623 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 625..632 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 633..636 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 639..642 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 643..645 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 651..664 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 669..676 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 679..686 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 700..703 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 707..713 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 725..728 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 737..744 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 746..751 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 756..761 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 769..773 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 775..777 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 781..785 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 787..796 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 823..826 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 830..832 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 844..846 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 848..854 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 856..861 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 866..868 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 882..886 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 889..893 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 898..902 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 909..920 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 921..923 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 925..930 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 933..935 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 939..949 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 962..971 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 974..976 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 977..981 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 982..985 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 986..992 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 994..997 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 1002..1004 FT /evidence="ECO:0007829|PDB:8FG8" FT HELIX 1019..1021 FT /evidence="ECO:0007829|PDB:8FG8" FT STRAND 1022..1026 FT /evidence="ECO:0007829|PDB:8FG8" FT TURN 1039..1042 FT /evidence="ECO:0007829|PDB:8FG8" SQ SEQUENCE 1476 AA; 165847 MW; 9C6E09F731B4CBCF CRC64; MDKKVRYKLR KVKKRWVTVS VASAVMTLTT LSGGLVKADS NESKSQISND SNTSVVTANE ESNVTTEVTS KQEAASSQTN HTVTTISSST SVVNPKEVVS NPYTVGETAS NGEKLQNQTT TVDKTSEAAA NNISKQTTEA DTDVIDDSNA ANLQILEKLP NVKEIDGKYY YYDNNGKVRT NFTLIADGKI LHFDETGAYT DTSIDTVNKD IVTTRSNLYK KYNQVYDRSA QSFEHVDHYL TAESWYRPKY ILKDGKTWTQ STEKDFRPLL MTWWPSQETQ RQYVNYMNAQ LGINKTYDDT SNQLQLNIAA ATIQAKIEAK ITTLKNTDWL RQTISAFVKT QSAWNSDSEK PFDDHLQNGA VLYDNEGKLT PYANSNYRIL NRTPTNQTGK KDPRYTADNT IGGYEFLLAN DVDNSNPVVQ AEQLNWLHFL MNFGNIYAND PDANFDSIRV DAVDNVDADL LQIAGDYLKA AKGIHKNDKA ANDHLSILEA WSDNDTPYLH DDGDNMINMD NKLRLSLLFS LAKPLNQRSG MNPLITNSLV NRTDDNAETA AVPSYSFIRA HDSEVQDLIR DIIKAEINPN VVGYSFTMEE IKKAFEIYNK DLLATEKKYT HYNTALSYAL LLTNKSSVPR VYYGDMFTDD GQYMAHKTIN YEAIETLLKA RIKYVSGGQA MRNQQVGNSE IITSVRYGKG ALKATDTGDR TTRTSGVAVI EGNNPSLRLK ASDRVVVNMG AAHKNQAYRP LLLTTDNGIK AYHSDQEAAG LVRYTNDRGE LIFTAADIKG YANPQVSGYL GVWVPVGAAA DQDVRVAAST APSTDGKSVH QNAALDSRVM FEGFSNFQAF ATKKEEYTNV VIAKNVDKFA EWGVTDFEMA PQYVSSTDGS FLDSVIQNGY AFTDRYDLGI SKPNKYGTAD DLVKAIKALH SKGIKVMADW VPDQMYAFPE KEVVTATRVD KFGKPVEGSQ IKSVLYVADS KSSGKDQQAK YGGAFLEELQ AKYPELFARK QISTGVPMDP SVKIKQWSAK YFNGTNILGR GAGYVLKDQA TNTYFNISDN KEINFLPKTL LNQDSQVGFS YDGKGYVYYS TSGYQAKNTF ISEGDKWYYF DNNGYMVTGA QSINGVNYYF LSNGLQLRDA ILKNEDGTYA YYGNDGRRYE NGYYQFMSGV WRHFNNGEMS VGLTVIDGQV QYFDEMGYQA KGKFVTTADG KIRYFDKQSG NMYRNRFIEN EEGKWLYLGE DGAAVTGSQT INGQHLYFRA NGVQVKGEFV TDRYGRISYY DSNSGDQIRN RFVRNAQGQW FYFDNNGYAV TGARTINGQH LYFRANGVQV KGEFVTDRHG RISYYDGNSG DQIRNRFVRN AQGQWFYFDN NGYAVTGART INGQHLYFRA NGVQVKGEFV TDRYGRISYY DSNSGDQIRN RFVRNAQGQW FYFDNNGYAV TGARTINGQH LYFRANGVQV KGEFVTDRYG RISYYDANSG ERVRIN //