ID G5JPW7_STRCG Unreviewed; 1461 AA.
AC G5JPW7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=STRCR_1701 {ECO:0000313|EMBL:EHI73776.1};
OS Streptococcus criceti HS-6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873449 {ECO:0000313|EMBL:EHI73776.1, ECO:0000313|Proteomes:UP000004322};
RN [1] {ECO:0000313|EMBL:EHI73776.1, ECO:0000313|Proteomes:UP000004322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-6 {ECO:0000313|EMBL:EHI73776.1,
RC ECO:0000313|Proteomes:UP000004322};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (JUL-2011) 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:EHI73776.1}.
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DR EMBL; AEUV02000002; EHI73776.1; -; Genomic_DNA.
DR RefSeq; WP_004226184.1; NZ_AEUV02000002.1.
DR STRING; 873449.STRCR_1701; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR OrthoDB; 2032428at2; -.
DR Proteomes; UP000004322; 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; 3.20.20.470; Glucansucrase; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR027636; Glucan-bd_rpt.
DR InterPro; IPR003318; Glyco_hydro70cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR022263; KxYKxGKxW.
DR NCBIfam; TIGR04035; glucan_65_rpt; 4.
DR NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR Pfam; PF01473; Choline_bind_1; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EHI73776.1}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..1461
FT /note="dextransucrase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003479406"
FT DOMAIN 246..1052
FT /note="Glycoside hydrolase family 70 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02324"
FT REPEAT 1436..1455
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 58..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1461 AA; 161503 MW; 82D6FFFCC17703F3 CRC64;
MEKNVHYKMH KVKKRWVTIS VASATMLASA LGASVASADT DAAAADANNA ANAAVAGDQA
ASSQDNQAAP LPATATSEDT GSTEEVAVNQ DAQVANTDTQ EAKWVPNTDN NSEISDAAVA
AADVQSVPQA LTNLSNVKQV DGKYYYYDAD GNVKKNFAIS VGDAIFYFDE TGAYKDTSKV
GADKTSSSAN QTTATFAANN RAYSTAAENF EAIDNYLTAD SWYRPKSILK DGKTWTESTK
DDFRPLLMAW WPDTETKRNY VNYMNKVVGI DKTYTAETSQ ADLTAAAELV QARIEQRITS
EKNTKWLREA ISAFVKTQPQ WNGESEKPYD DHLQNGALKF DNETSLTPDT QSGYRILNRT
PTNQTGSLDP RFTFNQNDPL GGYEYLLAND VDNSNPVVQA ESLNWLHYLL NFGSIYANDP
EANFDSIRVD AVDNVDADLL QISSDYLKSA YKIDKNNKNA NDHVSIVEAW SDNDTPYLHD
EGDNLMNMDN KFRLSMLWSL AKPLDKRSGL NPLIHNSVVD REVDDREVEK IPSYSFARAH
DSEVQDLIRD IIKAEINPNS FGYSFTQEEI DQAFKIYNED LKKTNKKYTH YNVPLSYTLL
LTNKGSIPRI YYGDMFTDDG QYMANKTVNY NAIESLLKAR MKYVSGGQAM QNYQIGNGEI
LTSVRYGKGA LKQSDKGDAT TRTSGIGIVM GNQPNFSLEG KVVALNMGAA HANQEYRALM
VSTKDGVATY ATDADASKAG MTKRTDENGY LYFLNDDLKG VANPQISGFL QVWVPVGAPA
DQDIRVAATN AASTDGKSLH QDAAMDSRVM FEGFSNFQAF ATKEDEYANV VIAKNVDKFV
SWGITDFEMA PQYTSSDDGQ FLDSVIQNGY AFTDRYDLGM SKANKYGTAE HLVKAIKALH
KAGLKVMADW VPDQMYTFPK KEVVTVTRTD KFGKPVAGSQ INHTLYVTDT KGSGDDYQAK
YGGAFLDELK EKYPELFTKK QISTGQAIDP SVKIKQWSAK YFNGSNILGR GANYVLSDQA
SNKYFNVAEG KVFLPGAMLG KVVESGIRFD GKGYIYNSST TGEQVKDSFI TEAGNLYYFG
KDGYMVMGAQ NIQGANYYFL ANGAALRNSI LTDQDGKSHY YANDGKRYEN GYYQFGNDSW
RYFENGVMAV GVTRVAGHDQ YFDKDGIQAK NKIIVTRDGK VRYFDEHNGN AVTNTFISDQ
AGHWYYLGKD GVAVTGAQTV GKQHLYFEAN GQQVKGDFVT AKDGKLYFFD GDSGDMWTDT
FVQDKTGHWF YLGKDGAAVT GAQTVRGQKL YFKANGQQVK GDIVKGADGK IRYYDANSGD
QVYNRTVKGS DGKTYIIGKD GVAITQTIAK GQTIKDGSVL RFYSMEGQLV TGSGWYSNAK
GQWLYVKNGQ VLTGLQTVGS QRVYFDANGI QAKGKAVRTS DGKLRYFDAN SGSMITNQWK
EVNGQYYYFD NNGVAIYRGW N
//
