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Q03174 (FRUA_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 120. 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:
Fructan beta-fructosidase

EC=3.2.1.80
Alternative name(s):
Exo-beta-D-fructosidase
Fructanase
Gene names
Name:fruA
Ordered Locus Names:SMU_78
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length1423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Subcellular location

Secretedcell wall; Peptidoglycan-anchor Potential.

Induction

By sucrose, fructan substrates and fructose.

Sequence similarities

Belongs to the glycosyl hydrolase 32 family.

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMPeptidoglycan-anchor
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionfructan beta-fructosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Chain40 – 13911352Fructan beta-fructosidase
PRO_0000033406
Propeptide1392 – 142332Removed by sortase Potential
PRO_0000033407

Regions

Region455 – 4584Substrate binding By similarity
Region513 – 5142Substrate binding By similarity
Region581 – 5822Substrate binding By similarity
Region867 – 8715Involved in binding of sugars with beta-(2,6) linkages or binding of molecular weight fructans By similarity
Motif1388 – 13925LPXTG sorting signal Potential

Sites

Active site4581 By similarity
Binding site4741Substrate By similarity
Binding site7831Substrate By similarity

Amino acid modifications

Modified residue13911Pentaglycyl murein peptidoglycan amidated threonine Potential

Experimental info

Sequence conflict781G → E in AAA26889. Ref.1
Sequence conflict2801I → V in AAA26889. Ref.1
Sequence conflict9421S → T in AAA26889. Ref.1
Sequence conflict10021T → I in AAA26889. Ref.1
Sequence conflict12901N → S in AAA26889. Ref.1
Sequence conflict13841P → S in AAA26889. Ref.1
Sequence conflict14161G → S in AAA26889. Ref.1
Sequence conflict14211R → S in AAA26889. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q03174 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 03FF85E42535ABCA

FASTA1,423158,660
        10         20         30         40         50         60 
MEEETVCKNW FMRKSGKSWI FGCAVFFVLG LATALPVAAE EISQTTAADT AVTEVRTEDS 

        70         80         90        100        110        120 
SQTSSQETAV TETTQSEGTA SKQLTTPAVA DQTTEPTDNE PISSSDGASS PYQVTDTTEP 

       130        140        150        160        170        180 
QQTLTPADSE PQAKADVQQA AAPKKEEINP VTNLEDMSHD TNGTWEVRED GIHSNAIGKG 

       190        200        210        220        230        240 
DSFLYSQSSG KNFVYATDVT FKQNSGAAAL VFRSNNDSNN KNMYAVNVDI GGHKAKFWRW 

       250        260        270        280        290        300 
VDNKDIQLID ERDVVPTADN RYTLKVVAVN NWISYYVNDI LMASTGDYVL QKADKGQNTV 

       310        320        330        340        350        360 
IPEGHFGLLN WNGDMVFQNT KFALLDDTTA PLIDNITVRS DRGNVEKQGQ FFSEEPLHIQ 

       370        380        390        400        410        420 
YVSNDASQVS LDIAKHNPAA TVTVEDKTGR VYTDPSHLPV NVGANYFTVK STVIDSFGRT 

       430        440        450        460        470        480 
VTLTYRINVH RRQNDEVYYN ELYRDQYHYS VKDGWANDPN GLVYYNGVYH LFHQFYDDTK 

       490        500        510        520        530        540 
WGPMHWAHAT STDLIHWKEE PIAFYPDSNG YMFSGCVVVD EHNSSGLFKT AKGGLVAIIT 

       550        560        570        580        590        600 
ANGNGQRMEL AYSEDEGKTW QKYDRIVADW SNDPLQNQDF RDPKVFHWNN QWFMVLAGGP 

       610        620        630        640        650        660 
LRIYSSNNLK DWKVESTYPD LHTECPDMYP IVANDGVLKW VLSRGGRFYK VGDFKQVDGK 

       670        680        690        700        710        720 
WTFIADDAYK DKDQVMNFGK DSYAAMTYYV HDFGTETRPT IPKLTEVNWM NTWEDYCNLV 

       730        740        750        760        770        780 
ADTVGQDFNG TFNLNLDLGL INENGQYILT QTPVKAYDSL RDVNTALHFK DVTVDANNTL 

       790        800        810        820        830        840 
LKDFKGDSYE IVSHFRPDEK TTKVGFNLRV GNGQATKVIY DLQTETLSID RSQSGTILSA 

       850        860        870        880        890        900 
AFAKVNSQHV TKNADGSIDL HIYVDRASVE VFSKNNTVAG ANQIFPNPEA VGASIIVEGG 

       910        920        930        940        950        960 
KAQADISVYQ MKTIWTDKKD TAKPVAMNTT TAKELALQVG QSQDLQVYLA PASVRQDVEW 

       970        980        990       1000       1010       1020 
TISDPSLVRT SQKGNVLHLT AVKKGKLTIT AISKENPSLS KTFTISITLN NFKTNLKGLQ 

      1030       1040       1050       1060       1070       1080 
SVTGKWYVDD ETLYDSNTSS NDYYMASQKP GFKEYDYDID LKYQRGLINL FVASGNIDPS 

      1090       1100       1110       1120       1130       1140 
QAYSVQFGDS ETVRLYRFAG DTIAEANMGK RINDDQYHHI KVTKTKNSII ISVDGQEVMS 

      1150       1160       1170       1180       1190       1200 
HNFDQVDSYF NDAYVGLGLW DGAVEFQNFF VTDHATTPKP DSDPTPQPDA PEALAQEREL 

      1210       1220       1230       1240       1250       1260 
IDPATGVRVI LQKGELASIV RVKVSHIETN DAHTPAVLNA KDYDLFNITP IDKNEKVVAI 

      1270       1280       1290       1300       1310       1320 
TKPATVLLPI DAGKVVDKVV YLPNTDKEEN LPFTIVSLTD SNGKKQSYVR FTAEHFSEYG 

      1330       1340       1350       1360       1370       1380 
LVYQAENQTN LKSKEKQDNV AISYPLNLEQ EVKVSSISRK YAANKTADVN SVQQTEPSVM 

      1390       1400       1410       1420 
SSSPKATLPD TGDHKTDLSQ LGVLAMIGSF LVEIAGYFKK RKD 

« Hide

References

« Hide 'large scale' references
[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]"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
U78296 Genomic DNA. Translation: AAA26889.1.
AE014133 Genomic DNA. Translation: AAN57863.1.
PIRA49206.
RefSeqNP_720557.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ03174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.78.

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Protocols and materials databases

DNASU1029658.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN57863; AAN57863; SMU_78.
GeneID1029658.
KEGGsmu:SMU_78.
PATRIC19662427. VBIStrMut61772_0067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1621.
KOK03332.
OMASYAAMTY.
OrthoDBEOG6DJXZ4.
ProtClustDBCLSK907841.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-91-MONOMER.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
2.60.120.200. 1 hit.
2.60.120.560. 1 hit.
InterProIPR003343. Big_2.
IPR025883. Cadherin-like_b_sandwich.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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]
PfamPF02368. 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]
SMARTSM00635. BID_2. 1 hit.
SM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMSSF49373. SSF49373. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF75005. SSF75005. 1 hit.
TIGRFAMsTIGR03715. KxYKxGKxW. 1 hit.
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRUA_STRMU
AccessionPrimary (citable) accession number: Q03174
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: February 19, 2014
This is version 120 of the entry and version 2 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