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Reviewed, UniProtKB/Swiss-Prot P39653 (DEXT_STRDO)

Last modified February 9, 2010. Version 61. 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

Names and origin

Protein namesRecommended name:
    Dextranase
    EC=3.2.1.11
Alternative name(s):
    Alpha-1,6-glucan-6-glucanohydrolase
Gene names
Name: dex
Encoded onPlasmid pYA902
OrganismStreptococcus downei (Streptococcus sobrinus)
Taxonomic identifier1317 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length1337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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.

Subcellular location

Secretedcell wall; Peptidoglycan-anchor Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 66 family.

Caution

It is uncertain whether Met-1 or Met-5 is the initiator.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.3.

Temperature dependence:

Optimum temperature is 39 degrees Celsius.

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMPeptidoglycan-anchor
   Technical termDirect protein sequencing
Plasmid
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from electronic annotation. Source: InterPro

cell wall

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondextranase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.1
Chain31 – 13081278Dextranase
PRO_0000012236
Propeptide1309 – 133729Removed by sortase Potential
PRO_0000012237

Regions

Motif1305 – 13095LPXTG sorting signal Potential

Amino acid modifications

Modified residue13081Pentaglycyl murein peptidoglycan amidated threonine Potential

Sequences

Sequence LengthMass (Da)Tools
P39653-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B494275A77A2E3D0

FASTA1,337143,298
        10         20         30         40         50         60 
MNNRMLSFPS MLFLLAFGIV LSVSAGTTHA DELANQTAKV ADEASIVVST SQAAVEQTQS 

        70         80         90        100        110        120 
QEKEISPAME EDTSNLSLKP NAQQESQSPD SSTELQDPAE QTPPETSDAS APATTSADSV 

       130        140        150        160        170        180 
EKYAQDATQN QSSTSNGPGV IRATSAQVTA TRSVVSSQSG DAIVDLSADK ASYRQGEDVN 

       190        200        210        220        230        240 
LSVDFKNTTD KEQDVTVYAD VYYIDNKLGT YKFSKHLKAG EGYKMQSGDL KIPASQFENN 

       250        260        270        280        290        300 
HGYLLKVRVR DADNNTLSEV NKAIAVESDW TKFPRYGIVG GSQDTNNSLL SKDADRYRAE 

       310        320        330        340        350        360 
IEKMKNMNIN SYFFYDVYKT ATNPFPSDEA TFKQDWNTWS GSEIDTQAVK DIVNQVHDGG 

       370        380        390        400        410        420 
AVAMLYNMIL AENTNTGEAP VLPETEYAYN SDDRGYGAQG QPMSYTVKIP KDGQEEDVEI 

       430        440        450        460        470        480 
QRYYNPTSKL WQDYIADKMG QAMKNGGFDG WQGDTIGDNE VYSYADKDSN DPSKKFWLTE 

       490        500        510        520        530        540 
GYAEFLRAIK EKLPNYYLTV NDVNGEQIYR LKDGNQDVIY NEIWPFGPAL PSEMAAVKPN 

       550        560        570        580        590        600 
TVTSRPVLTK VRQGDWKISI VGAYMEGSEN GGSKADAEAG KSLQTDAVLL TSASIAAAGG 

       610        620        630        640        650        660 
YHMSLAALAN QQDETDGGQG IGVLQTAYYP TQSLKTSSEL TRKNNDYQQF ITAYENVLRD 

       670        680        690        700        710        720 
GVENDDAQVN TFDSNGQKLS TDAKGITGNQ VWTYGKKGDN FRTVQLLNLM GINSDWKNED 

       730        740        750        760        770        780 
GSAANKTPDE QTNLTVKYAL GDVSMEDAQR MANQTYVTSP DDWSKSNLQK VSASVKTDEN 

       790        800        810        820        830        840 
GKPVLVINVP KLTLWDVVYI SNANQESAPE ADQAQTPAAQ SSDDKVAENE TSQPAAEDAK 

       850        860        870        880        890        900 
EQTSEPAQDQ AAPAEQGQAI NQAESPATEP EAEVTPATAE PAKVDAPEAN QAADQAVSPE 

       910        920        930        940        950        960 
PASQEQAASQ SQPEANQTPA SNETPATQGN SEQPELNEPT AQTQPSSQVS PANTSVTPVA 

       970        980        990       1000       1010       1020 
EQPTNQGQAA DKADQAPTNS TSTPESTSPV EPAATDQSSD TPIVTAGNLS VQPAETETPT 

      1030       1040       1050       1060       1070       1080 
VPDKQGDSKA NQSSTETPVA DQVPAVAEQP QATEPNQAKP SVDKAAAPEA LSLIQLKQQT 

      1090       1100       1110       1120       1130       1140 
PAIQAKEADD PEVDETKSEV TPDSGTDKAP EAGQVDSDKA PTVKPSTPEN NDNQPNNAND 

      1150       1160       1170       1180       1190       1200 
ADKNKTNEAD SNKANQDSTK GSSADQSGKS TTPEDGPDNS SPEDPETKPS DPNTDTSDQE 

      1210       1220       1230       1240       1250       1260 
QVKPSLPVVP NQTVDDPKTD DTDTPANTDS AKSKKVADAD KNKVATDSEG RQKSSEFPKE 

      1270       1280       1290       1300       1310       1320 
ATDLEKVGQP ASPQVAGVKS SVATSPEKKS EPVSKTSTTS SSDKLPKTGD HKTVVLIIVL 

      1330 
GLVFVGMTGL LARHEKK 

« Hide

References

[1]"Purification and characterization of Streptococcus sobrinus dextranase produced in recombinant Escherichia coli and sequence analysis of the dextranase gene."
Wanda S.-Y., Curtiss R. III
J. Bacteriol. 176:3839-3850(1994) [PubMed: 8021165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-36.
Strain: 6715 / UAB66.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96978 Genomic DNA. Translation: AAA21772.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH66. Glycoside Hydrolase Family 66.

Enzyme and pathway databases

BRENDA3.2.1.11. 290403.

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...

Entry information

Entry nameDEXT_STRDO
AccessionPrimary (citable) accession number: P39653
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 9, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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