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Protein

Dextranase

Gene

dexA

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

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
Proteomesi
  • UP000002512 Componenti: Chromosome

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000012238? – 814Dextranase
Signal peptidei1 – ?
PropeptideiPRO_0000012239815 – 850Removed by sortasePROSITE-ProRule annotationAdd BLAST36

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei814Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

Keywords - PTMi

Peptidoglycan-anchor

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi210007.SMU_2042.

Structurei

Secondary structure

1850
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi109 – 111Combined sources3
Beta strandi113 – 115Combined sources3
Beta strandi121 – 124Combined sources4
Beta strandi126 – 128Combined sources3
Beta strandi131 – 133Combined sources3
Beta strandi135 – 145Combined sources11
Beta strandi148 – 159Combined sources12
Beta strandi164 – 166Combined sources3
Beta strandi171 – 174Combined sources4
Beta strandi181 – 192Combined sources12
Beta strandi198 – 208Combined sources11
Beta strandi218 – 221Combined sources4
Helixi225 – 227Combined sources3
Helixi233 – 235Combined sources3
Helixi236 – 248Combined sources13
Beta strandi253 – 256Combined sources4
Beta strandi269 – 274Combined sources6
Turni279 – 281Combined sources3
Beta strandi284 – 286Combined sources3
Helixi287 – 299Combined sources13
Beta strandi303 – 314Combined sources12
Helixi323 – 325Combined sources3
Beta strandi328 – 333Combined sources6
Beta strandi343 – 346Combined sources4
Beta strandi349 – 355Combined sources7
Helixi360 – 377Combined sources18
Beta strandi381 – 385Combined sources5
Beta strandi391 – 393Combined sources3
Helixi395 – 397Combined sources3
Helixi403 – 405Combined sources3
Helixi409 – 411Combined sources3
Helixi413 – 423Combined sources11
Beta strandi427 – 431Combined sources5
Helixi434 – 436Combined sources3
Helixi439 – 442Combined sources4
Beta strandi448 – 453Combined sources6
Beta strandi458 – 460Combined sources3
Beta strandi463 – 467Combined sources5
Helixi470 – 484Combined sources15
Beta strandi488 – 491Combined sources4
Beta strandi505 – 507Combined sources3
Helixi508 – 514Combined sources7
Helixi521 – 534Combined sources14
Beta strandi537 – 539Combined sources3
Beta strandi541 – 543Combined sources3
Helixi547 – 549Combined sources3
Beta strandi558 – 560Combined sources3
Helixi570 – 585Combined sources16
Helixi587 – 591Combined sources5
Beta strandi602 – 604Combined sources3
Beta strandi621 – 629Combined sources9
Beta strandi631 – 640Combined sources10
Beta strandi647 – 649Combined sources3
Helixi653 – 655Combined sources3
Beta strandi663 – 671Combined sources9
Helixi677 – 684Combined sources8
Beta strandi686 – 690Combined sources5
Turni694 – 698Combined sources5
Beta strandi700 – 702Combined sources3
Beta strandi705 – 709Combined sources5
Beta strandi715 – 732Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VMNX-ray1.60A100-732[»]
3VMOX-ray1.90A100-732[»]
3VMPX-ray1.88A100-732[»]
SMRiQ54443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi811 – 815LPXTG sorting signalPROSITE-ProRule annotation5

Sequence similaritiesi

Belongs to the glycosyl hydrolase 66 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107PMM. Bacteria.
ENOG410XS5X. LUCA.
KOiK05988.
OMAiENDSAEP.

Family and domain databases

CDDicd14745. GH66. 1 hit.
InterProiIPR025092. Glyco_hydro_66.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti16A → N (PubMed:8657012).Curated1
Sequence conflicti16A → N (PubMed:8535521).Curated1
Sequence conflicti22T → A (PubMed:8657012).Curated1
Sequence conflicti22T → A (PubMed:8535521).Curated1
Sequence conflicti39V → A (PubMed:8657012).Curated1
Sequence conflicti39V → A (PubMed:8535521).Curated1
Sequence conflicti56G → E (PubMed:8657012).Curated1
Sequence conflicti56G → E (PubMed:8535521).Curated1
Sequence conflicti67S → P (PubMed:8657012).Curated1
Sequence conflicti67S → P (PubMed:8535521).Curated1
Sequence conflicti141A → V (PubMed:8657012).Curated1
Sequence conflicti141A → V (PubMed:8535521).Curated1
Sequence conflicti376N → T (PubMed:8657012).Curated1
Sequence conflicti376N → T (PubMed:8535521).Curated1
Sequence conflicti504V → I (PubMed:8657012).Curated1
Sequence conflicti504V → I (PubMed:8535521).Curated1
Sequence conflicti704A → T (PubMed:8657012).Curated1
Sequence conflicti704A → T (PubMed:8535521).Curated1
Sequence conflicti707I → V (PubMed:8657012).Curated1
Sequence conflicti707I → V (PubMed:8535521).Curated1
Sequence conflicti776 – 778VDE → EDG (PubMed:8657012).Curated3
Sequence conflicti776 – 778VDE → EDG (PubMed:8535521).Curated3
Sequence conflicti783I → L (PubMed:8657012).Curated1
Sequence conflicti783I → L (PubMed:8535521).Curated1
Sequence conflicti849K → N (PubMed:8657012).Curated1
Sequence conflicti849K → N (PubMed:8535521).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VMNX-ray1.60A100-732[»]
3VMOX-ray1.90A100-732[»]
3VMPX-ray1.88A100-732[»]
SMRiQ54443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_2042.

Protein family/group databases

CAZyiGH66. Glycoside Hydrolase Family 66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107PMM. Bacteria.
ENOG410XS5X. LUCA.
KOiK05988.
OMAiENDSAEP.

Enzyme and pathway databases

BRENDAi3.2.1.11. 5941.

Family and domain databases

CDDicd14745. GH66. 1 hit.
InterProiIPR025092. Glyco_hydro_66.
[Graphical view]
PfamiPF13199. Glyco_hydro_66. 1 hit.
[Graphical view]
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.