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Reviewed, UniProtKB/Swiss-Prot Q54443 (DEXT_STRMU)

Last modified June 16, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dextranase
    EC=3.2.1.11
Alternative name(s):
    Alpha-1,6-glucan-6-glucanohydrolase
Gene names
Name: dexA
Ordered Locus Names: SMU_2042
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

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Protein attributes

Sequence length850 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

May play a role in sucrose-independent adherence to the pellicle-coated tooth surface.

Catalytic activity

Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted › cell wall; Peptidoglycan-anchor Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 66 family.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell surface

Inferred from electronic annotation. Source: InterPro

cell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondextranase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ?
Chain? – 814DextranasePRO_0000012238
Propeptide815 – 85036Removed by sortase Potential
PRO_0000012239

Regions

Motif811 – 8155LPXTG sorting signal Potential

Amino acid modifications

Modified residue8141Pentaglycyl murein peptidoglycan amidated threonine Potential

Experimental info

Sequence conflict161A → N Ref.1
Sequence conflict161A → N Ref.2
Sequence conflict221T → A Ref.1
Sequence conflict221T → A Ref.2
Sequence conflict391V → A Ref.1
Sequence conflict391V → A Ref.2
Sequence conflict561G → E Ref.1
Sequence conflict561G → E Ref.2
Sequence conflict671S → P Ref.1
Sequence conflict671S → P Ref.2
Sequence conflict1411A → V Ref.1
Sequence conflict1411A → V Ref.2
Sequence conflict3761N → T Ref.1
Sequence conflict3761N → T Ref.2
Sequence conflict5041V → I Ref.1
Sequence conflict5041V → I Ref.2
Sequence conflict7041A → T Ref.1
Sequence conflict7041A → T Ref.2
Sequence conflict7071I → V Ref.1
Sequence conflict7071I → V Ref.2
Sequence conflict776 – 7783VDE → EDG Ref.1
Sequence conflict776 – 7783VDE → EDG Ref.2
Sequence conflict7831I → L Ref.1
Sequence conflict7831I → L Ref.2
Sequence conflict8491K → N Ref.1
Sequence conflict8491K → N Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q54443-1 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: FCF3E7DF7B4EA178

FASTA85094,482
        10         20         30         40         50         60 
MEQSNRQTAE PAIRSAETVD STINSFQETD LKVQEKEDVA AAVQTESASI DSNEQGQSVS 

        70         80         90        100        110        120 
ANTNTQSQAK KLSNNSHQEP MQMVSAANKE RAVLETAQNQ KNGNMINLTT DKAVYQAGEA 

       130        140        150        160        170        180 
VHLNLTLNNT TSLAQNITAT AEVYSLENKL KTLQYTKYLL PNESYTTQKG EFVIPANSLA 

       190        200        210        220        230        240 
NNRGYLLKVN ISDSQNNILE QGNRAIAVED DWRTFPRYAA IGGSQKDNNS VLTKNLPDYY 

       250        260        270        280        290        300 
RELEQMKNMN INSYFFYDVY KSATNPFPNV PKFDQSWNWW SHSQVETDAV KALVNRVHQT 

       310        320        330        340        350        360 
GAVAMLYNMI LAQNANETAV LPDTEYIYNY ETGGYGQNGQ VMTYSIDDKP LQYYYNPLSK 

       370        380        390        400        410        420 
SWQNYISNAM AQAMKNGGFD GWQGDTIGDN RVLSHNQKDS RDIAHSFMLS DVYAEFLNKM 

       430        440        450        460        470        480 
KEKLPQYYLT LNDVNGENIS KLANSKQDVI YNELWPFGTS ALGNRPQESY GDLKARVDQV 

       490        500        510        520        530        540 
RQATGKSLIV GAYMEEPKFD DNRVPLNGAA RDVLASATYQ TDAVLLTTAA IAAAGGYHMS 

       550        560        570        580        590        600 
LAALANPNDG GGVGVLETAY YPTQSLKVSK ELNRKNYHYQ QFITAYENLL RDKVENDSAE 

       610        620        630        640        650        660 
PQTFTANGRQ LSQDALGING DQVWTYAKKG NDFRTIQLLN LMGITSDWKN EDGYENNKTP 

       670        680        690        700        710        720 
DEQTNLLVTY PLTGVSMAEA DRIAKQVYLT SPDDWLQSSM ISLATQIKTN ENGDPVLYIQ 

       730        740        750        760        770        780 
VPRLTLWDMI YINETIKPET PKVPEQPQHP ARTLEPAIPQ TPEAVSPLPV ANKQAVDENK 

       790        800        810        820        830        840 
NEIVSALTGE ENDLQLPTLS KRSLSISQAE LPQTGDNNET RSNLLKVIGA GALLIGAAGL 

       850 
LSLIKGRKKD

« Hide

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References

« Hide 'large scale' references
[1]"Sequence analysis of the Streptococcus mutans Ingbritt dexA gene encoding extracellular dextranase."
Igarashi T., Yamamoto A., Goto N.
Microbiol. Immunol. 39:853-860(1995) [PubMed: 8657012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Ingbritt.
[2]"Insertional inactivation of the Streptococcus mutans dexA (dextranase) gene results in altered adherence and dextran catabolism."
Colby S.M., Whiting G.C., Tao L., Russell R.R.B.
Microbiology 141:2929-2936(1995) [PubMed: 8535521] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Ingbritt.
[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: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.

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Cross-references

Sequence databases

D49430 Genomic DNA. Translation: BAA08409.1.
AE014133 Genomic DNA. Translation: AAN59642.1.
RefSeqNP_722336.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH66. Glycoside Hydrolase Family 66.

Genome annotation databases

GeneID1029395.
GenomeReviewsGene locus SMU_2042 in contig AE014133_GR.
KEGGsmu:SMU.2042.
NMPDRfig|210007.1.peg.1849.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ54443.

Enzyme and pathway databases

BioCycSMUT210007:SMU_2042-MON.
BRENDA3.2.1.11. 20716.

Family and domain databases

InterProIPR019931. LPXTG-motif_cell_wall_anchor.
IPR001899. Surface_protein_Gram_pos_cocci.
[Graphical view]
TIGRFAMsTIGR01167. LPXTG_anchor. 1 hit.
PROSITEPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDEXT_STRMU
AccessionPrimary (citable) accession number: Q54443
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents