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Q54443

- DEXT_STRMU

UniProt

Q54443 - DEXT_STRMU

Protein

Dextranase

Gene

dexA

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (28 Nov 2002)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    GO - Molecular functioni

    1. dextranase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciSMUT210007:GC7Z-1929-MONOMER.
    BRENDAi3.2.1.11. 5941.

    Protein family/group databases

    CAZyiGH66. Glycoside Hydrolase Family 66.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dextranase (EC:3.2.1.11)
    Alternative name(s):
    Alpha-1,6-glucan-6-glucanohydrolase
    Gene namesi
    Name:dexA
    Ordered Locus Names:SMU_2042
    OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
    Taxonomic identifieri210007 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000002512: Chromosome

    Subcellular locationi

    Secretedcell wall PROSITE-ProRule annotation; Peptidoglycan-anchor PROSITE-ProRule annotation

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell wall, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 814DextranasePRO_0000012238
    Signal peptidei1 – ?
    Propeptidei815 – 85036Removed by sortasePROSITE-ProRule annotationPRO_0000012239Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei814 – 8141Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

    Keywords - PTMi

    Peptidoglycan-anchor

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi210007.SMU.2042.

    Structurei

    Secondary structure

    1
    850
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi109 – 1113
    Beta strandi113 – 1153
    Beta strandi121 – 1244
    Beta strandi126 – 1283
    Beta strandi131 – 1333
    Beta strandi135 – 14511
    Beta strandi148 – 15912
    Beta strandi164 – 1663
    Beta strandi171 – 1744
    Beta strandi181 – 19212
    Beta strandi198 – 20811
    Beta strandi218 – 2214
    Helixi225 – 2273
    Helixi233 – 2353
    Helixi236 – 24813
    Beta strandi253 – 2564
    Beta strandi269 – 2746
    Turni279 – 2813
    Beta strandi284 – 2863
    Helixi287 – 29913
    Beta strandi303 – 31412
    Helixi323 – 3253
    Beta strandi328 – 3336
    Beta strandi343 – 3464
    Beta strandi349 – 3557
    Helixi360 – 37718
    Beta strandi381 – 3855
    Beta strandi391 – 3933
    Helixi395 – 3973
    Helixi403 – 4053
    Helixi409 – 4113
    Helixi413 – 42311
    Beta strandi427 – 4315
    Helixi434 – 4363
    Helixi439 – 4424
    Beta strandi448 – 4536
    Beta strandi458 – 4603
    Beta strandi463 – 4675
    Helixi470 – 48415
    Beta strandi488 – 4914
    Beta strandi505 – 5073
    Helixi508 – 5147
    Helixi521 – 53414
    Beta strandi537 – 5393
    Beta strandi541 – 5433
    Helixi547 – 5493
    Beta strandi558 – 5603
    Helixi570 – 58516
    Helixi587 – 5915
    Beta strandi602 – 6043
    Beta strandi621 – 6299
    Beta strandi631 – 64010
    Beta strandi647 – 6493
    Helixi653 – 6553
    Beta strandi663 – 6719
    Helixi677 – 6848
    Beta strandi686 – 6905
    Turni694 – 6985
    Beta strandi700 – 7023
    Beta strandi705 – 7095
    Beta strandi715 – 73218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VMNX-ray1.60A100-732[»]
    3VMOX-ray1.90A100-732[»]
    3VMPX-ray1.88A100-732[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi811 – 8155LPXTG sorting signalPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 66 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG47856.
    KOiK05988.
    OMAiNANETAV.
    OrthoDBiEOG651SQZ.

    Family and domain databases

    InterProiIPR025092. Glyco_hydro_66.
    IPR019931. LPXTG_anchor.
    [Graphical view]
    PfamiPF13199. Glyco_hydro_66. 1 hit.
    [Graphical view]
    PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q54443-1 [UniParc]FASTAAdd to Basket

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    MEQSNRQTAE PAIRSAETVD STINSFQETD LKVQEKEDVA AAVQTESASI    50
    DSNEQGQSVS ANTNTQSQAK KLSNNSHQEP MQMVSAANKE RAVLETAQNQ 100
    KNGNMINLTT DKAVYQAGEA VHLNLTLNNT TSLAQNITAT AEVYSLENKL 150
    KTLQYTKYLL PNESYTTQKG EFVIPANSLA NNRGYLLKVN ISDSQNNILE 200
    QGNRAIAVED DWRTFPRYAA IGGSQKDNNS VLTKNLPDYY RELEQMKNMN 250
    INSYFFYDVY KSATNPFPNV PKFDQSWNWW SHSQVETDAV KALVNRVHQT 300
    GAVAMLYNMI LAQNANETAV LPDTEYIYNY ETGGYGQNGQ VMTYSIDDKP 350
    LQYYYNPLSK SWQNYISNAM AQAMKNGGFD GWQGDTIGDN RVLSHNQKDS 400
    RDIAHSFMLS DVYAEFLNKM KEKLPQYYLT LNDVNGENIS KLANSKQDVI 450
    YNELWPFGTS ALGNRPQESY GDLKARVDQV RQATGKSLIV GAYMEEPKFD 500
    DNRVPLNGAA RDVLASATYQ TDAVLLTTAA IAAAGGYHMS LAALANPNDG 550
    GGVGVLETAY YPTQSLKVSK ELNRKNYHYQ QFITAYENLL RDKVENDSAE 600
    PQTFTANGRQ LSQDALGING DQVWTYAKKG NDFRTIQLLN LMGITSDWKN 650
    EDGYENNKTP DEQTNLLVTY PLTGVSMAEA DRIAKQVYLT SPDDWLQSSM 700
    ISLATQIKTN ENGDPVLYIQ VPRLTLWDMI YINETIKPET PKVPEQPQHP 750
    ARTLEPAIPQ TPEAVSPLPV ANKQAVDENK NEIVSALTGE ENDLQLPTLS 800
    KRSLSISQAE LPQTGDNNET RSNLLKVIGA GALLIGAAGL LSLIKGRKKD 850
    Length:850
    Mass (Da):94,482
    Last modified:November 28, 2002 - v2
    Checksum:iFCF3E7DF7B4EA178
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161A → N(PubMed:8657012)Curated
    Sequence conflicti16 – 161A → N(PubMed:8535521)Curated
    Sequence conflicti22 – 221T → A(PubMed:8657012)Curated
    Sequence conflicti22 – 221T → A(PubMed:8535521)Curated
    Sequence conflicti39 – 391V → A(PubMed:8657012)Curated
    Sequence conflicti39 – 391V → A(PubMed:8535521)Curated
    Sequence conflicti56 – 561G → E(PubMed:8657012)Curated
    Sequence conflicti56 – 561G → E(PubMed:8535521)Curated
    Sequence conflicti67 – 671S → P(PubMed:8657012)Curated
    Sequence conflicti67 – 671S → P(PubMed:8535521)Curated
    Sequence conflicti141 – 1411A → V(PubMed:8657012)Curated
    Sequence conflicti141 – 1411A → V(PubMed:8535521)Curated
    Sequence conflicti376 – 3761N → T(PubMed:8657012)Curated
    Sequence conflicti376 – 3761N → T(PubMed:8535521)Curated
    Sequence conflicti504 – 5041V → I(PubMed:8657012)Curated
    Sequence conflicti504 – 5041V → I(PubMed:8535521)Curated
    Sequence conflicti704 – 7041A → T(PubMed:8657012)Curated
    Sequence conflicti704 – 7041A → T(PubMed:8535521)Curated
    Sequence conflicti707 – 7071I → V(PubMed:8657012)Curated
    Sequence conflicti707 – 7071I → V(PubMed:8535521)Curated
    Sequence conflicti776 – 7783VDE → EDG(PubMed:8657012)Curated
    Sequence conflicti776 – 7783VDE → EDG(PubMed:8535521)Curated
    Sequence conflicti783 – 7831I → L(PubMed:8657012)Curated
    Sequence conflicti783 – 7831I → L(PubMed:8535521)Curated
    Sequence conflicti849 – 8491K → N(PubMed:8657012)Curated
    Sequence conflicti849 – 8491K → N(PubMed:8535521)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49430 Genomic DNA. Translation: BAA08409.1.
    AE014133 Genomic DNA. Translation: AAN59642.1.
    RefSeqiNP_722336.1. NC_004350.2.
    WP_011074684.1. NC_004350.2.

    Genome annotation databases

    EnsemblBacteriaiAAN59642; AAN59642; SMU_2042.
    GeneIDi1029395.
    KEGGismu:SMU_2042.
    PATRICi19666043. VBIStrMut61772_1820.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49430 Genomic DNA. Translation: BAA08409.1 .
    AE014133 Genomic DNA. Translation: AAN59642.1 .
    RefSeqi NP_722336.1. NC_004350.2.
    WP_011074684.1. NC_004350.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VMN X-ray 1.60 A 100-732 [» ]
    3VMO X-ray 1.90 A 100-732 [» ]
    3VMP X-ray 1.88 A 100-732 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 210007.SMU.2042.

    Protein family/group databases

    CAZyi GH66. Glycoside Hydrolase Family 66.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN59642 ; AAN59642 ; SMU_2042 .
    GeneIDi 1029395.
    KEGGi smu:SMU_2042.
    PATRICi 19666043. VBIStrMut61772_1820.

    Phylogenomic databases

    eggNOGi NOG47856.
    KOi K05988.
    OMAi NANETAV.
    OrthoDBi EOG651SQZ.

    Enzyme and pathway databases

    BioCyci SMUT210007:GC7Z-1929-MONOMER.
    BRENDAi 3.2.1.11. 5941.

    Family and domain databases

    InterProi IPR025092. Glyco_hydro_66.
    IPR019931. LPXTG_anchor.
    [Graphical view ]
    Pfami PF13199. Glyco_hydro_66. 1 hit.
    [Graphical view ]
    PROSITEi PS50847. GRAM_POS_ANCHORING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Ingbritt.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700610 / UA159.

    Entry informationi

    Entry nameiDEXT_STRMU
    AccessioniPrimary (citable) accession number: Q54443
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 28, 2002
    Last modified: October 1, 2014
    This is version 96 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3