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P08987 (GTFB_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucosyltransferase-I

Short name=GTF-I
EC=2.4.1.5
Alternative name(s):
Dextransucrase
Sucrose 6-glucosyltransferase
Gene names
Name:gtfB
Ordered Locus Names:SMU_1004
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length1476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris.

Catalytic activity

Sucrose + ((1->6)-alpha-D-glucosyl)(n) = D-fructose + ((1->6)-alpha-D-glucosyl)(n+1).

Subcellular location

Secreted.

Miscellaneous

GTF-I synthesizes water-insoluble glucans (alpha 1,3-linked glucose and some 1,6 linkages), GTF-S synthesizes water-soluble glucans (alpha 1,6-glucose). GTF-SI synthesizes both forms of glucans.

Sequence similarities

Belongs to the glycosyl hydrolase 70 family.

Contains 13 cell wall-binding repeats.

Ontologies

Keywords
   Cellular componentSecreted
   DiseaseDental caries
   DomainRepeat
Signal
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglucan biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondextransucrase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glucosyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 14761442Glucosyltransferase-I
PRO_0000021385

Regions

Repeat159 – 17820Cell wall-binding 1
Repeat179 – 19921Cell wall-binding 2
Repeat1087 – 110620Cell wall-binding 3
Repeat1107 – 112620Cell wall-binding 4
Repeat1170 – 118920Cell wall-binding 5
Repeat1214 – 123421Cell wall-binding 6
Repeat1235 – 125420Cell wall-binding 7
Repeat1279 – 129921Cell wall-binding 8
Repeat1300 – 131920Cell wall-binding 9
Repeat1344 – 136421Cell wall-binding 10
Repeat1365 – 138420Cell wall-binding 11
Repeat1409 – 142921Cell wall-binding 12
Repeat1430 – 144920Cell wall-binding 13
Region200 – 1051852Catalytic; approximate

Natural variations

Natural variant621S → T in strain: MT4239.
Natural variant651T → I in strain: GS-5.
Natural variant681V → A in strain: GS-5, MT4245, MT4251, MT4467 and MT8148.
Natural variant781Q → P in strain: MT4251.
Natural variant861I → S in strain: GS-5, MT4245, MT4251, MT4467 and MT8148.
Natural variant891S → F in strain: MT4251.
Natural variant1681K → N in strain: MT4251.
Natural variant2761S → D in strain: GS-5, MT4467 and MT8148.
Natural variant3991N → R in strain: MT4239.
Natural variant4741I → T in strain: MT4239.
Natural variant5121K → R in strain: MT8148.
Natural variant5191F → Y in strain: MT8148.
Natural variant7011T → I in strain: MT8148.
Natural variant7081A → V in strain: MT8148.
Natural variant9381F → L in strain: MT8148.
Natural variant952 – 9576FGKPVE → YGTPVA in strain: GS-5, MT4239 and MT4467.
Natural variant963 – 9642SV → NT in strain: GS-5, MT4239 and MT4467.
Natural variant968 – 9703ADS → VDG in strain: GS-5, MT4239 and MT4467.
Natural variant10861A → T in strain: MT4239.
Natural variant11581S → N in strain: MT4239.
Natural variant11631H → Y in strain: MT4251.
Natural variant11681E → K in strain: MT8148.
Natural variant11821Y → C in strain: MT8148.
Natural variant12341A → P in strain: MT4239.
Natural variant12631R → H in strain: GS-5 and MT4467.
Natural variant12631R → P in strain: MT8148.
Natural variant12641Y → H in strain: GS-5, MT4239, MT4467 and MT8148.
Natural variant12721S → G in strain: GS-5, MT4239, MT4467 and MT8148.
Natural variant13291H → Y in strain: GS-5 and MT4467.
Natural variant13941Y → H in strain: GS-5, MT4239, MT4467 and MT8148.
Natural variant14021S → G in strain: GS-5, MT4239, MT4467 and MT8148.
Natural variant14591Y → H in strain: MT4467.

Experimental info

Sequence conflict5701R → A in AAA88588. Ref.1
Sequence conflict800 – 81718ADQDV…STDGK → LIKMFALRLARPHQQMA in AAA88588. Ref.1
Sequence conflict13101H → L in AAA88588. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P08987 [UniParc].

Last modified December 6, 2002. Version 3.
Checksum: 9C6E09F731B4CBCF

FASTA1,476165,847
        10         20         30         40         50         60 
MDKKVRYKLR KVKKRWVTVS VASAVMTLTT LSGGLVKADS NESKSQISND SNTSVVTANE 

        70         80         90        100        110        120 
ESNVTTEVTS KQEAASSQTN HTVTTISSST SVVNPKEVVS NPYTVGETAS NGEKLQNQTT 

       130        140        150        160        170        180 
TVDKTSEAAA NNISKQTTEA DTDVIDDSNA ANLQILEKLP NVKEIDGKYY YYDNNGKVRT 

       190        200        210        220        230        240 
NFTLIADGKI LHFDETGAYT DTSIDTVNKD IVTTRSNLYK KYNQVYDRSA QSFEHVDHYL 

       250        260        270        280        290        300 
TAESWYRPKY ILKDGKTWTQ STEKDFRPLL MTWWPSQETQ RQYVNYMNAQ LGINKTYDDT 

       310        320        330        340        350        360 
SNQLQLNIAA ATIQAKIEAK ITTLKNTDWL RQTISAFVKT QSAWNSDSEK PFDDHLQNGA 

       370        380        390        400        410        420 
VLYDNEGKLT PYANSNYRIL NRTPTNQTGK KDPRYTADNT IGGYEFLLAN DVDNSNPVVQ 

       430        440        450        460        470        480 
AEQLNWLHFL MNFGNIYAND PDANFDSIRV DAVDNVDADL LQIAGDYLKA AKGIHKNDKA 

       490        500        510        520        530        540 
ANDHLSILEA WSDNDTPYLH DDGDNMINMD NKLRLSLLFS LAKPLNQRSG MNPLITNSLV 

       550        560        570        580        590        600 
NRTDDNAETA AVPSYSFIRA HDSEVQDLIR DIIKAEINPN VVGYSFTMEE IKKAFEIYNK 

       610        620        630        640        650        660 
DLLATEKKYT HYNTALSYAL LLTNKSSVPR VYYGDMFTDD GQYMAHKTIN YEAIETLLKA 

       670        680        690        700        710        720 
RIKYVSGGQA MRNQQVGNSE IITSVRYGKG ALKATDTGDR TTRTSGVAVI EGNNPSLRLK 

       730        740        750        760        770        780 
ASDRVVVNMG AAHKNQAYRP LLLTTDNGIK AYHSDQEAAG LVRYTNDRGE LIFTAADIKG 

       790        800        810        820        830        840 
YANPQVSGYL GVWVPVGAAA DQDVRVAAST APSTDGKSVH QNAALDSRVM FEGFSNFQAF 

       850        860        870        880        890        900 
ATKKEEYTNV VIAKNVDKFA EWGVTDFEMA PQYVSSTDGS FLDSVIQNGY AFTDRYDLGI 

       910        920        930        940        950        960 
SKPNKYGTAD DLVKAIKALH SKGIKVMADW VPDQMYAFPE KEVVTATRVD KFGKPVEGSQ 

       970        980        990       1000       1010       1020 
IKSVLYVADS KSSGKDQQAK YGGAFLEELQ AKYPELFARK QISTGVPMDP SVKIKQWSAK 

      1030       1040       1050       1060       1070       1080 
YFNGTNILGR GAGYVLKDQA TNTYFNISDN KEINFLPKTL LNQDSQVGFS YDGKGYVYYS 

      1090       1100       1110       1120       1130       1140 
TSGYQAKNTF ISEGDKWYYF DNNGYMVTGA QSINGVNYYF LSNGLQLRDA ILKNEDGTYA 

      1150       1160       1170       1180       1190       1200 
YYGNDGRRYE NGYYQFMSGV WRHFNNGEMS VGLTVIDGQV QYFDEMGYQA KGKFVTTADG 

      1210       1220       1230       1240       1250       1260 
KIRYFDKQSG NMYRNRFIEN EEGKWLYLGE DGAAVTGSQT INGQHLYFRA NGVQVKGEFV 

      1270       1280       1290       1300       1310       1320 
TDRYGRISYY DSNSGDQIRN RFVRNAQGQW FYFDNNGYAV TGARTINGQH LYFRANGVQV 

      1330       1340       1350       1360       1370       1380 
KGEFVTDRHG RISYYDGNSG DQIRNRFVRN AQGQWFYFDN NGYAVTGART INGQHLYFRA 

      1390       1400       1410       1420       1430       1440 
NGVQVKGEFV TDRYGRISYY DSNSGDQIRN RFVRNAQGQW FYFDNNGYAV TGARTINGQH 

      1450       1460       1470 
LYFRANGVQV KGEFVTDRYG RISYYDANSG ERVRIN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the gtfB gene from Streptococcus mutans."
Shiroza T., Ueda S., Kuramitsu H.K.
J. Bacteriol. 169:4263-4270(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GS-5.
[2]"Molecular analyses of glucosyltransferase genes among strains of Streptococcus mutans."
Fujiwara T., Terao Y., Hoshino T., Kawabata S., Ooshima T., Sobue S., Kimura S., Hamada S.
FEMS Microbiol. Lett. 161:331-336(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MT4239 / Serotype c, MT4245 / Serotype e, MT4251 / Serotype f, MT4467 / Serotype e and MT8148 / Serotype c.
[3]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17361 Genomic DNA. Translation: AAA88588.1.
D88651 Genomic DNA. Translation: BAA26101.1.
D88654 Genomic DNA. Translation: BAA26105.1.
D88657 Genomic DNA. Translation: BAA26109.1.
D88660 Genomic DNA. Translation: BAA26113.1.
D89977 Genomic DNA. Translation: BAA26119.1.
AE014133 Genomic DNA. Translation: AAN58705.1.
PIRB33135.
RefSeqNP_721399.1. NC_004350.2.

3D structure databases

ProteinModelPortalP08987.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.1004.

Protein family/group databases

CAZyGH70. Glycoside Hydrolase Family 70.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58705; AAN58705; SMU_1004.
GeneID1028336.
KEGGsmu:SMU_1004.
PATRIC19664129. VBIStrMut61772_0897.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5263.
KOK00689.
OMAANGVQVK.
OrthoDBEOG60PH6T.
ProtClustDBCLSK907891.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-955-MONOMER.
SABIO-RKP08987.

Family and domain databases

Gene3D3.20.20.80. 3 hits.
InterProIPR018337. Cell_wall/Cho-bd_repeat.
IPR027636. Glucan-bd_rpt.
IPR003318. Glyco_hydro70cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR022263. KxYKxGKxW.
[Graphical view]
PfamPF01473. CW_binding_1. 4 hits.
PF02324. Glyco_hydro_70. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 4 hits.
TIGRFAMsTIGR04035. glucan_65_rpt. 6 hits.
TIGR03715. KxYKxGKxW. 1 hit.
PROSITEPS51170. CW. 13 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGTFB_STRMU
AccessionPrimary (citable) accession number: P08987
Secondary accession number(s): O69381 expand/collapse secondary AC list , O69384, O69387, O69390, O69396
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 6, 2002
Last modified: December 11, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries