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Q03174

- FRUA_STRMU

UniProt

Q03174 - FRUA_STRMU

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Protein

Fructan beta-fructosidase

Gene

fruA

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

This protein is a fructanase enzyme which degrades levans and inulins to fructose and also cleaves sucrose into glucose and fructose and can therefore function as an extracellular invertase.

Catalytic activityi

Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei458 – 4581PROSITE-ProRule annotation
Binding sitei474 – 4741SubstrateBy similarity
Binding sitei783 – 7831SubstrateBy similarity

GO - Molecular functioni

  1. fructan beta-fructosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-91-MONOMER.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructan beta-fructosidase (EC:3.2.1.80)
Alternative name(s):
Exo-beta-D-fructosidase
Fructanase
Gene namesi
Name:fruA
Ordered Locus Names:SMU_78
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002512: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence AnalysisAdd
BLAST
Chaini40 – 13911352Fructan beta-fructosidasePRO_0000033406Add
BLAST
Propeptidei1392 – 142332Removed by sortaseSequence AnalysisPRO_0000033407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1391 – 13911Pentaglycyl murein peptidoglycan amidated threonineSequence Analysis

Keywords - PTMi

Peptidoglycan-anchor

Expressioni

Inductioni

By sucrose, fructan substrates and fructose.

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU.78.

Structurei

3D structure databases

ProteinModelPortaliQ03174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni455 – 4584Substrate bindingBy similarity
Regioni513 – 5142Substrate bindingBy similarity
Regioni581 – 5822Substrate bindingBy similarity
Regioni867 – 8715Involved in binding of sugars with beta-(2,6) linkages or binding of molecular weight fructansBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1388 – 13925LPXTG sorting signalSequence Analysis

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1621.
KOiK03332.
OMAiSYAAMTY.
OrthoDBiEOG6DJXZ4.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
2.60.120.200. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR003343. Big_2.
IPR025883. Cadherin-like_b_sandwich.
IPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR008964. Invasin/intimin_cell_adhesion.
IPR022263. KxYKxGKxW.
IPR001791. Laminin_G.
IPR011040. Sialidases.
[Graphical view]
PfamiPF02368. Big_2. 1 hit.
PF12733. Cadherin-like. 1 hit.
PF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
SMARTiSM00635. BID_2. 1 hit.
SM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49373. SSF49373. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF75005. SSF75005. 1 hit.
TIGRFAMsiTIGR03715. KxYKxGKxW. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q03174-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEETVCKNW FMRKSGKSWI FGCAVFFVLG LATALPVAAE EISQTTAADT
60 70 80 90 100
AVTEVRTEDS SQTSSQETAV TETTQSEGTA SKQLTTPAVA DQTTEPTDNE
110 120 130 140 150
PISSSDGASS PYQVTDTTEP QQTLTPADSE PQAKADVQQA AAPKKEEINP
160 170 180 190 200
VTNLEDMSHD TNGTWEVRED GIHSNAIGKG DSFLYSQSSG KNFVYATDVT
210 220 230 240 250
FKQNSGAAAL VFRSNNDSNN KNMYAVNVDI GGHKAKFWRW VDNKDIQLID
260 270 280 290 300
ERDVVPTADN RYTLKVVAVN NWISYYVNDI LMASTGDYVL QKADKGQNTV
310 320 330 340 350
IPEGHFGLLN WNGDMVFQNT KFALLDDTTA PLIDNITVRS DRGNVEKQGQ
360 370 380 390 400
FFSEEPLHIQ YVSNDASQVS LDIAKHNPAA TVTVEDKTGR VYTDPSHLPV
410 420 430 440 450
NVGANYFTVK STVIDSFGRT VTLTYRINVH RRQNDEVYYN ELYRDQYHYS
460 470 480 490 500
VKDGWANDPN GLVYYNGVYH LFHQFYDDTK WGPMHWAHAT STDLIHWKEE
510 520 530 540 550
PIAFYPDSNG YMFSGCVVVD EHNSSGLFKT AKGGLVAIIT ANGNGQRMEL
560 570 580 590 600
AYSEDEGKTW QKYDRIVADW SNDPLQNQDF RDPKVFHWNN QWFMVLAGGP
610 620 630 640 650
LRIYSSNNLK DWKVESTYPD LHTECPDMYP IVANDGVLKW VLSRGGRFYK
660 670 680 690 700
VGDFKQVDGK WTFIADDAYK DKDQVMNFGK DSYAAMTYYV HDFGTETRPT
710 720 730 740 750
IPKLTEVNWM NTWEDYCNLV ADTVGQDFNG TFNLNLDLGL INENGQYILT
760 770 780 790 800
QTPVKAYDSL RDVNTALHFK DVTVDANNTL LKDFKGDSYE IVSHFRPDEK
810 820 830 840 850
TTKVGFNLRV GNGQATKVIY DLQTETLSID RSQSGTILSA AFAKVNSQHV
860 870 880 890 900
TKNADGSIDL HIYVDRASVE VFSKNNTVAG ANQIFPNPEA VGASIIVEGG
910 920 930 940 950
KAQADISVYQ MKTIWTDKKD TAKPVAMNTT TAKELALQVG QSQDLQVYLA
960 970 980 990 1000
PASVRQDVEW TISDPSLVRT SQKGNVLHLT AVKKGKLTIT AISKENPSLS
1010 1020 1030 1040 1050
KTFTISITLN NFKTNLKGLQ SVTGKWYVDD ETLYDSNTSS NDYYMASQKP
1060 1070 1080 1090 1100
GFKEYDYDID LKYQRGLINL FVASGNIDPS QAYSVQFGDS ETVRLYRFAG
1110 1120 1130 1140 1150
DTIAEANMGK RINDDQYHHI KVTKTKNSII ISVDGQEVMS HNFDQVDSYF
1160 1170 1180 1190 1200
NDAYVGLGLW DGAVEFQNFF VTDHATTPKP DSDPTPQPDA PEALAQEREL
1210 1220 1230 1240 1250
IDPATGVRVI LQKGELASIV RVKVSHIETN DAHTPAVLNA KDYDLFNITP
1260 1270 1280 1290 1300
IDKNEKVVAI TKPATVLLPI DAGKVVDKVV YLPNTDKEEN LPFTIVSLTD
1310 1320 1330 1340 1350
SNGKKQSYVR FTAEHFSEYG LVYQAENQTN LKSKEKQDNV AISYPLNLEQ
1360 1370 1380 1390 1400
EVKVSSISRK YAANKTADVN SVQQTEPSVM SSSPKATLPD TGDHKTDLSQ
1410 1420
LGVLAMIGSF LVEIAGYFKK RKD
Length:1,423
Mass (Da):158,660
Last modified:November 28, 2002 - v2
Checksum:i03FF85E42535ABCA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781G → E in AAA26889. (PubMed:1398976)Curated
Sequence conflicti280 – 2801I → V in AAA26889. (PubMed:1398976)Curated
Sequence conflicti942 – 9421S → T in AAA26889. (PubMed:1398976)Curated
Sequence conflicti1002 – 10021T → I in AAA26889. (PubMed:1398976)Curated
Sequence conflicti1290 – 12901N → S in AAA26889. (PubMed:1398976)Curated
Sequence conflicti1384 – 13841P → S in AAA26889. (PubMed:1398976)Curated
Sequence conflicti1416 – 14161G → S in AAA26889. (PubMed:1398976)Curated
Sequence conflicti1421 – 14211R → S in AAA26889. (PubMed:1398976)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U78296 Genomic DNA. Translation: AAA26889.1.
AE014133 Genomic DNA. Translation: AAN57863.1.
PIRiA49206.
RefSeqiNP_720557.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN57863; AAN57863; SMU_78.
GeneIDi1029658.
KEGGismu:SMU_78.
PATRICi19662427. VBIStrMut61772_0067.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U78296 Genomic DNA. Translation: AAA26889.1 .
AE014133 Genomic DNA. Translation: AAN57863.1 .
PIRi A49206.
RefSeqi NP_720557.1. NC_004350.2.

3D structure databases

ProteinModelPortali Q03174.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 210007.SMU.78.

Protein family/group databases

CAZyi GH32. Glycoside Hydrolase Family 32.

Protocols and materials databases

DNASUi 1029658.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN57863 ; AAN57863 ; SMU_78 .
GeneIDi 1029658.
KEGGi smu:SMU_78.
PATRICi 19662427. VBIStrMut61772_0067.

Phylogenomic databases

eggNOGi COG1621.
KOi K03332.
OMAi SYAAMTY.
OrthoDBi EOG6DJXZ4.

Enzyme and pathway databases

BioCyci SMUT210007:GC7Z-91-MONOMER.

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
2.60.120.200. 1 hit.
2.60.120.560. 1 hit.
InterProi IPR003343. Big_2.
IPR025883. Cadherin-like_b_sandwich.
IPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR008964. Invasin/intimin_cell_adhesion.
IPR022263. KxYKxGKxW.
IPR001791. Laminin_G.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF02368. Big_2. 1 hit.
PF12733. Cadherin-like. 1 hit.
PF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view ]
SMARTi SM00635. BID_2. 1 hit.
SM00640. Glyco_32. 1 hit.
[Graphical view ]
SUPFAMi SSF49373. SSF49373. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF75005. SSF75005. 1 hit.
TIGRFAMsi TIGR03715. KxYKxGKxW. 1 hit.
PROSITEi PS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the Streptococcus mutans GS-5 fruA gene encoding exo-beta-D-fructosidase."
    Burne R.A., Penders J.E.C.
    Infect. Immun. 60:4621-4632(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: GS-5.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700610 / UA159.

Entry informationi

Entry nameiFRUA_STRMU
AccessioniPrimary (citable) accession number: Q03174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: October 29, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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