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Q54443

- DEXT_STRMU

UniProt

Q54443 - DEXT_STRMU

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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

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
Complete GO annotation...

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-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
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

« Hide

        10         20         30         40         50
MEQSNRQTAE PAIRSAETVD STINSFQETD LKVQEKEDVA AAVQTESASI
60 70 80 90 100
DSNEQGQSVS ANTNTQSQAK KLSNNSHQEP MQMVSAANKE RAVLETAQNQ
110 120 130 140 150
KNGNMINLTT DKAVYQAGEA VHLNLTLNNT TSLAQNITAT AEVYSLENKL
160 170 180 190 200
KTLQYTKYLL PNESYTTQKG EFVIPANSLA NNRGYLLKVN ISDSQNNILE
210 220 230 240 250
QGNRAIAVED DWRTFPRYAA IGGSQKDNNS VLTKNLPDYY RELEQMKNMN
260 270 280 290 300
INSYFFYDVY KSATNPFPNV PKFDQSWNWW SHSQVETDAV KALVNRVHQT
310 320 330 340 350
GAVAMLYNMI LAQNANETAV LPDTEYIYNY ETGGYGQNGQ VMTYSIDDKP
360 370 380 390 400
LQYYYNPLSK SWQNYISNAM AQAMKNGGFD GWQGDTIGDN RVLSHNQKDS
410 420 430 440 450
RDIAHSFMLS DVYAEFLNKM KEKLPQYYLT LNDVNGENIS KLANSKQDVI
460 470 480 490 500
YNELWPFGTS ALGNRPQESY GDLKARVDQV RQATGKSLIV GAYMEEPKFD
510 520 530 540 550
DNRVPLNGAA RDVLASATYQ TDAVLLTTAA IAAAGGYHMS LAALANPNDG
560 570 580 590 600
GGVGVLETAY YPTQSLKVSK ELNRKNYHYQ QFITAYENLL RDKVENDSAE
610 620 630 640 650
PQTFTANGRQ LSQDALGING DQVWTYAKKG NDFRTIQLLN LMGITSDWKN
660 670 680 690 700
EDGYENNKTP DEQTNLLVTY PLTGVSMAEA DRIAKQVYLT SPDDWLQSSM
710 720 730 740 750
ISLATQIKTN ENGDPVLYIQ VPRLTLWDMI YINETIKPET PKVPEQPQHP
760 770 780 790 800
ARTLEPAIPQ TPEAVSPLPV ANKQAVDENK NEIVSALTGE ENDLQLPTLS
810 820 830 840 850
KRSLSISQAE LPQTGDNNET RSNLLKVIGA GALLIGAAGL LSLIKGRKKD
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.

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.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 97 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