ID W3Y948_9STRE Unreviewed; 1493 AA.
AC W3Y948;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=dextransucrase {ECO:0000256|ARBA:ARBA00012592};
DE EC=2.4.1.5 {ECO:0000256|ARBA:ARBA00012592};
DE AltName: Full=Dextransucrase {ECO:0000256|ARBA:ARBA00029911};
DE AltName: Full=Sucrose 6-glucosyltransferase {ECO:0000256|ARBA:ARBA00032238};
GN ORFNames=HMPREF1519_0806 {ECO:0000313|EMBL:ETS94041.1};
OS Streptococcus sp. SR4.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1161417 {ECO:0000313|EMBL:ETS94041.1, ECO:0000313|Proteomes:UP000019059};
RN [1] {ECO:0000313|EMBL:ETS94041.1, ECO:0000313|Proteomes:UP000019059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR4 {ECO:0000313|EMBL:ETS94041.1,
RC ECO:0000313|Proteomes:UP000019059};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Production of extracellular glucans, that are thought to play
CC a key role in the development of the dental plaque because of their
CC ability to adhere to smooth surfaces and mediate the aggregation of
CC bacterial cells and food debris. {ECO:0000256|ARBA:ARBA00003243}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->6)-alpha-D-glucosyl](n) + sucrose = [(1->6)-alpha-D-
CC glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:18825, Rhea:RHEA-
CC COMP:11144, Rhea:RHEA-COMP:11145, ChEBI:CHEBI:17992,
CC ChEBI:CHEBI:18269, ChEBI:CHEBI:37721; EC=2.4.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001152};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 70 family.
CC {ECO:0000256|ARBA:ARBA00009247}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETS94041.1}.
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DR EMBL; AZYW01000010; ETS94041.1; -; Genomic_DNA.
DR RefSeq; WP_022495764.1; NZ_AZYW01000010.1.
DR PATRIC; fig|1161417.3.peg.339; -.
DR Proteomes; UP000019059; Unassembled WGS sequence.
DR GO; GO:0047849; F:dextransucrase activity; IEA:UniProtKB-EC.
DR GO; GO:0046527; F:glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0009250; P:glucan biosynthetic process; IEA:InterPro.
DR Gene3D; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 4.
DR Gene3D; 2.30.30.420; glucansucrase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR027636; Glucan-bd_rpt.
DR InterPro; IPR003318; Glyco_hydro70cat.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR022263; KxYKxGKxW.
DR NCBIfam; TIGR04035; glucan_65_rpt; 5.
DR NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR Pfam; PF19127; Choline_bind_3; 5.
DR Pfam; PF02324; Glyco_hydro_70; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF69360; Cell wall binding repeat; 4.
DR PROSITE; PS51170; CW; 1.
PE 3: Inferred from homology;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:ETS94041.1}.
FT DOMAIN 267..1063
FT /note="Glycoside hydrolase family 70 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02324"
FT REPEAT 1076..1095
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 66..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1493 AA; 166240 MW; 37173138869BC456 CRC64;
MGKKVHYKLH KVKKQWVTIA VTSAALASIV GGATVANQKV SADETTQPVA STTAESDVVV
ETHEVAAPAA TATTDATATT TDKAADTATV ETPAAVTTAA DTSANTVAPA TTDRAAVANG
ATTEAPAATA TATDTTLTVA EKPKSGVTEK EETAALSLDN IKQVDGKYYY VKEDGSYKTN
FAVSVNGQLL YFGKDGALTS TSTHSFTPGT TNLVDAFSSH NRAYDSKKES FELVDGYLTP
NSWYRPVTIL ENGEKWRVST EKDFRPLLMA WWPDVDTQVA YLNTFSKHFN LNATYSTSQS
QSELNAAAKT IQIKIEQEIS AKKSTEWLRQ AIESFVKEQD QWNTTTENYT LADHLQGGAL
LYVNNDKTPW ANSDYRLLNR TPSNQDGSLN GTGRYLGGYE FLLANDVDNS NPVVQAEQLN
QIHYLVNWGS IVMGDKDANF DGIRVDAVDN VDADLLQVYT NYFRAAFGVD KSEANALAHI
SILEAWDLND NAYNQKHDGA ALAMDNNLRY AIMGALYGSG SSLKDLITSS LTDRTNNSKY
GDTQANYIFA RAHDNLVQDI IRDIVQKEIN PKSDGYTMTD AELKRAFEIY NEDMKKAEKR
YTINNIPAAY ALILQNMEQV TRVYYGDLYT DNGQYMATKS PYYDAITTLL KNRMKYVSGG
QSMKVDTFNG KEILSSVRYG KDIMTADQTT GVAETSKHSG MLTLIANNQD FSLGDGTLKV
NMGKLHANQA YRPLLLGTDK GIVTYENDAA AAGKIKYTDA EGNLTFSGDE IKGYRTVDMR
GYLGVWVPVG APDNQDIRVK GSDKKLEKTF SATEALDSQV IYEGFSNFQD FVEKDSQYTN
KLIAENAELF KSWGITSFEM APQFVSADDR TFLDSVIQNG YAFTDRYDLA MSKNNKYGSK
EDLRDALKAL HKQGIQAIAD WVPDQLYQLP GQEVVTATRA NSYGTPKANA YINNTLYVAN
SKSSGKDFQA QYGGEFLDEL QKKYPQLFED VMISTGKKID PSVKIKQWSA KYMNGTNILG
RGSRYVLSND ATGRYYQVTE NGIFLPKPLT DQGGKTGFYY DGKGMAYFDN SGFQAKNAFI
KYAGNYYYFD KEGYMLTGRQ DIDGKTYFFL PNGIQLRDSI YQQDGKYYYF GSFGEQYKDG
YFVFDVPKEG TSETEAKFRY FSPTGEMAVG LTHAGGGLQY FDENGFQAKG TKYVTPDGKL
YFFDKNSGNA YTNRWAEIDG IWYEFNDQGY AQAKKGEFYT TDGSTWFYRD AAGKNVTGAL
TLDGHEYYFR ANGAQVKGEF VTENGKISYY TVDNGYKVKD KFFEVNGKWY HADKDGNLAT
GRQTIDHLNY YFNADGSQVK SDFFTLDGGK TWYYAKDNGE IVTGAYSIGG KNYYFKEDGS
QVKGDFVKNA DGSLSYYDKD SGERLNNRFL TTGNNVWYYF KDGKAVTGRQ NIDGKEYYFD
HLGRQVKGSP ISTPKGVEYY ESVLGERVTN TWITFQDGKT VFFDENGYAD FDK
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