GTFB_STRMU
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 03-AUG-2022, entry version 165.
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; Firmicutes; 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}.
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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 AlphaFoldDB; P08987; -.
DR SMR; P08987; -.
DR STRING; 210007.SMU_1004; -.
DR ChEMBL; CHEMBL3822351; -.
DR CAZy; GH70; Glycoside Hydrolase Family 70.
DR PRIDE; P08987; -.
DR ABCD; P08987; 3 sequenced antibodies.
DR EnsemblBacteria; AAN58705; AAN58705; SMU_1004.
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 OMA; QHLYFRA; -.
DR PhylomeDB; P08987; -.
DR SABIO-RK; P08987; -.
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 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; 1.
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; 6.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR PROSITE; PS51170; CW; 13.
PE 3: Inferred from homology;
KW Dental caries; Glycosyltransferase; Reference proteome; Repeat; Secreted;
KW 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"
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
