ID M4JBQ4_9STRE Unreviewed; 1462 AA.
AC M4JBQ4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 Name=gtfD {ECO:0000313|EMBL:AGC00423.1};
OS Streptococcus troglodytae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1111760 {ECO:0000313|EMBL:AGC00423.1};
RN [1] {ECO:0000313|EMBL:AGC00423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mark {ECO:0000313|EMBL:AGC00423.1};
RX PubMed=23457545;
RA Argimon S., Alekseyenko A.V., DeSalle R., Caufield P.W.;
RT "Phylogenetic analysis of glucosyltransferases and implications for the
RT coevolution of mutans streptococci with their Mammalian hosts.";
RL PLoS ONE 8:E56305-E56305(2013).
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}.
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DR EMBL; JX073016; AGC00423.1; -; Genomic_DNA.
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; 3.
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; PF01473; Choline_bind_1; 1.
DR Pfam; PF19127; Choline_bind_3; 4.
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; 3.
DR PROSITE; PS51170; CW; 5.
PE 3: Inferred from homology;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:AGC00423.1}.
FT DOMAIN 281..1103
FT /note="Glycoside hydrolase family 70 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02324"
FT REPEAT 1116..1136
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 1180..1201
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 1246..1266
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 1267..1286
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 1374..1394
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 37..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1462 AA; 163170 MW; 24B934680C354ED9 CRC64;
METKRRYKMH KVKKHWVTVA VTSSLITLSS TMLGVSASAE TESQTSDKVV TQKSEDDKAA
SESSQTDAQR SEQAQTAQTQ AQSQTSTVDS SPDGIKKTLS QNVTTEASSD DKTVTDAKAA
QSQTSAAQIE RAEEAQTSAS SQALTQAKAE QTKQRQTAAQ GNDTSVDLTT VPNVKQIDGK
YYYIGSDGQP KKNFALTVNN KVLYFDKNTG ALTDTSQYQF NQGLTKLNND YTPHNQIVNF
ENNSLETIDN YITADSWYRP KDILKDGKTW TASSESDLRP LLMSWWPDKQ TQIAYLNYMN
QQGLGTGENY TADSSQESLN LAAQTVQVKI ETKISQTKQT QWLRDIINSF VKTQPNWNSQ
TESDTSAGDK DHLQGGALLY SNSDKTAYAN SDYRLLNRTP TNQTGKPKYF EDNSSGGYDF
LLANDIDNSN PAVQAEQLNW LHYLMNYGSI VANDPEANFD GVRVDAVDNV NADLLQIASD
YLKAHYGVDK SEKNAIDHLS ILEAWSDNDP QYNKDTKGAQ LPIDNKLRLS LLYALTRPLE
KDASNKSEIR SGLEPVITNS LNNRSAEGKN SERMANYIFI RAHDSEVQTV IAKIIKAQIN
PKTDGLTFTL DELKQAFKIY NEDMRQAKKK YTQSNIPTAY ALMLSNKDSI TRLYYGDMYS
DDGQYMATKS PYYDAIDTLL KARIKYAAGG QDMKITYVEG DKSQMDWDYT GVLTSVRYGT
GANEAADKGN EATKTQGMAV ITSNNPSLKL NQNDKVIVNM GAAHKNQEYR PLLLTTKDGL
TSYTSDAAAK SLYRKTNDKG ELIFDSSDIQ GYLNPQVSGY LAVWVPVGAS DNQDVRVAAS
NKANATGQVY ESSTALDSQL IYEGFSNFQD FVTKDSDYTN KKIAQNIDLF KSWGVTSFEM
APQYVSSEDG SFLDSIIQNG YAFEDRYDLA MSKNNKYGSQ QDMINAVKAL HKGGIQVIAD
WVPDQIYNLP GKEVVTATRV NDYGEYRKDS EIKNTLYAAN TKSNGKDYQA KYGGAFLSEL
AAKYPSIFNR TQISNGKKID PSEKITAWKA KYFNGTNILG RGAGYVLKDN ASDKYFELKG
NQTYLPKQMT NKEASTGFVN DGNGMTFYST SGYQAKNSFI QDAKGNWYYF DNNGHMVYGL
QHLNGEVQYF LSNGVQLRES FLENADGSKN YFGHLGNRYS NGYYSFDNDS KWRYFDANGV
MAVGLKTING NTQYFDQDGY QVKGAWITDS DGKKRYFDDG SGNMAVNRFA NDQNGDWYYL
NSDGIALVGV QTIDGKTYYF GQDGKQIKGK IITDNGKLKY FLANSGELAR NIFATDSQNN
WYYFGSDGVA VTGSQTIAGK KLYFASDGKQ VKGSFVTYDG KVHYYHADSG ELQVNRFEAD
KDGNWYYLDS NGEALTGSQR INGQRIFFTR EGKQVKGDVA YDERGLLRYY DKNSGNMVYN
KVVTLANGRR IGIDRWGIAR YY
//
