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P27470

- GTF2_STRDO

UniProt

P27470 - GTF2_STRDO

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Protein

Glucosyltransferase-I

Gene
N/A
Organism
Streptococcus downei (Streptococcus sobrinus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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 activityi

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

GO - Molecular functioni

  1. dextransucrase activity Source: UniProtKB-EC
  2. glucosyltransferase activity Source: InterPro

GO - Biological processi

  1. glucan biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiGH70. Glycoside Hydrolase Family 70.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosyltransferase-I (EC:2.4.1.5)
Short name:
GTF-I
Alternative name(s):
Dextransucrase
Sucrose 6-glucosyltransferase
OrganismiStreptococcus downei (Streptococcus sobrinus)
Taxonomic identifieri1317 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Keywords - Diseasei

Dental caries

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence AnalysisAdd
BLAST
Chaini39 – 15921554Glucosyltransferase-IPRO_0000021384Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP27470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati151 – 17020Cell wall-binding 1Add
BLAST
Repeati172 – 19120Cell wall-binding 2Add
BLAST
Repeati1083 – 110220Cell wall-binding 3Add
BLAST
Repeati1103 – 112220Cell wall-binding 4Add
BLAST
Repeati1167 – 118620Cell wall-binding 5Add
BLAST
Repeati1211 – 123121Cell wall-binding 6Add
BLAST
Repeati1232 – 125120Cell wall-binding 7Add
BLAST
Repeati1276 – 129621Cell wall-binding 8Add
BLAST
Repeati1297 – 131620Cell wall-binding 9Add
BLAST
Repeati1411 – 143020Cell wall-binding 10Add
BLAST
Repeati1455 – 147420Cell wall-binding 11Add
BLAST
Repeati1523 – 154220Cell wall-binding 12Add
BLAST
Repeati1567 – 158620Cell wall-binding 13Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 1044845Catalytic; approximateAdd
BLAST
Regioni1093 – 1592500Glucan-binding; approximateAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 70 family.Curated
Contains 13 cell wall-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.20.20.80. 4 hits.
InterProiIPR018337. 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]
PfamiPF01473. CW_binding_1. 5 hits.
PF02324. Glyco_hydro_70. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 4 hits.
TIGRFAMsiTIGR04035. glucan_65_rpt. 5 hits.
TIGR03715. KxYKxGKxW. 1 hit.
PROSITEiPS51170. CW. 13 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27470-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEKNVRFKMH KVKKRWVTLS VASATMLASA LGASVASADT DTASDDSNQT
60 70 80 90 100
VVTGDQTTNN QATDQTSIAA TATSEQSAST DAATDQASAA EQTQGTTAST
110 120 130 140 150
DTAAQTTTNA NEAKWVPTEN ENQGFTDEML AEAKNVATAE SDSIPSDLAK
160 170 180 190 200
MSNVKQVDGK YYYYDQDGNV KKNFAVSVGD KIYYFDETGA YKDTSKVDAD
210 220 230 240 250
KSSSAVSQNA TIFAANNRAY STSAKNFEAV DNYLTADSWY RPKSILKDGK
260 270 280 290 300
TWTESGKDDF RPLLMAWWPD TETKRNYVNY MNKVVGIDKT YTAETSQADL
310 320 330 340 350
TAAAELVQAR IEQKITSENN TKWLREAISA FVKTQPQWNG ESEKPYDDHL
360 370 380 390 400
QNGALLFDNQ TDLTPDTQSN YRLLNRTPTN QTGSLDSRFT YNPNDPLGGY
410 420 430 440 450
DFLLANDVDN SNPVVQAEQL NWLHYLLNFG SIYANDADAN FDSIRVDAED
460 470 480 490 500
NVDADQLQIS SDYLKAAYGI DKNNKNANNH VSIVEAWSDN DTPYLHDDGD
510 520 530 540 550
NLMNMDNKFR LSMLWSLAKP TDVRSGLNPL IHNSLVDREV DDREVETVPS
560 570 580 590 600
YSFARAHDSE VQDIIRDIIK AEINPNSFGY SFTQEEIDQA FKIYNEDLKK
610 620 630 640 650
SDKKYTHYNV PLSYTLLLTN KGSIPRVYYG DMFTDDGQYM ANKTVNYDAI
660 670 680 690 700
ESLLKARMKY VAGGQAMQNY QIGNGEILTS VRYGKGALKQ SDKGDATTRT
710 720 730 740 750
SGVGVVMGNQ PNFSLDGKVV ALNMGAAHAN QEYRALMVST KDGVATYATD
760 770 780 790 800
ADASKAGLVK RTDENGYLYF LNDDLKGVAN PQVSGFLQVW VPVGAADDQD
810 820 830 840 850
IRVAASDTAS TDGKSLHQDA AMDSRVMFEG FSNFQSFATK EEEYTNVVIA
860 870 880 890 900
NNVDKFVSWG ITDFEMAPQY VSSTDGQFQD SVIQNGYAFT DRYDLGMSKA
910 920 930 940 950
NKYGTADQLV KAIKALHAKG LKVMADWVPD QMYTFPKQEV VTVTRTDKFG
960 970 980 990 1000
KPIAGSQINH SLYVTDTKSS GDDYQAKYGG AFLDELKEKY PELFTKKQMS
1010 1020 1030 1040 1050
TGQAIDPSVK IKQWSAKYFN GSNILGRGAD YVLSDQVSNK YFNVASDTLF
1060 1070 1080 1090 1100
LPSSLLGKVV ESGIRYDGKG YIYNSSATGD QVKASFITEA GNLYYFGKDG
1110 1120 1130 1140 1150
YMVTGAQTIN GANYFFLENG TALRNTIYTD AQGNSHYYAN DGKRYENENG
1160 1170 1180 1190 1200
YQQFGNDWRY FKDGNMAVGL TTVDGNVQYF DKDGVQAKDK IIVTRDGKVR
1210 1220 1230 1240 1250
YFDQHNGNAV TNTFIADKTG HWYYLGKDGV AVTGAQTVGK QKLYFEANGQ
1260 1270 1280 1290 1300
QVKGDFVTSD EGKLYFYDVD SGDMWTDTFI EDKAGNWFYL GKDGAAVTGA
1310 1320 1330 1340 1350
QTIRGQKLYF KANGQQVKGD IVKGTDGKIR YYDAKSGEQV FNKTVKAADG
1360 1370 1380 1390 1400
KTYVIGNDGV AVDPSVVKGQ TFKDASGALR FYNLKGQLVT GSGWYETANH
1410 1420 1430 1440 1450
DWVYIQSGKA LTGEQTINGQ HLYFKKDGHQ VKGQLVTGTD GKVRYYDANS
1460 1470 1480 1490 1500
GDQAFNKSVT VNGKTYYFGN DGTAQTAGNP KGQTFKDGSD IRFYSMEGQL
1510 1520 1530 1540 1550
VTGSGWYSNA QGQWLYVKNG KVLTGLQTVG SQRVYFDENG IQAKGKAVRT
1560 1570 1580 1590
SDGKIRYFDE NSGSMITNQW KEVNGRYYYF GNDGARIYRG WN
Length:1,592
Mass (Da):176,168
Last modified:August 1, 1992 - v1
Checksum:iBC0A66D079351ECF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90213 Genomic DNA. Translation: BAA14241.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90213 Genomic DNA. Translation: BAA14241.1 .

3D structure databases

ProteinModelPortali P27470.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH70. Glycoside Hydrolase Family 70.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.80. 4 hits.
InterProi IPR018337. 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 ]
Pfami PF01473. CW_binding_1. 5 hits.
PF02324. Glyco_hydro_70. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 4 hits.
TIGRFAMsi TIGR04035. glucan_65_rpt. 5 hits.
TIGR03715. KxYKxGKxW. 1 hit.
PROSITEi PS51170. CW. 13 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Peptide sequences for sucrose splitting and glucan binding within Streptococcus sobrinus glucosyltransferase (water-insoluble glucan synthetase)."
    Abo H., Matsumura T., Kodama T., Ohta H., Fukui K., Kato K., Kagawa H.
    J. Bacteriol. 173:989-996(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 6715 / Serotype G.

Entry informationi

Entry nameiGTF2_STRDO
AccessioniPrimary (citable) accession number: P27470
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3