ID B1N008_LEUCK Unreviewed; 2057 AA.
AC B1N008;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
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 OrderedLocusNames=LCK_01285 {ECO:0000313|EMBL:ACA83110.1};
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA83110.1, ECO:0000313|Proteomes:UP000002166};
RN [1] {ECO:0000313|EMBL:ACA83110.1, ECO:0000313|Proteomes:UP000002166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20 {ECO:0000313|EMBL:ACA83110.1,
RC ECO:0000313|Proteomes:UP000002166};
RX PubMed=18281406; DOI=10.1128/JB.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA83110.1; -; Genomic_DNA.
DR RefSeq; WP_012305377.1; NC_010471.1.
DR SMR; B1N008; -.
DR STRING; 349519.LCK_01285; -.
DR CAZy; GH70; Glycoside Hydrolase Family 70.
DR KEGG; lci:LCK_01285; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3757; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_001623_1_0_9; -.
DR OrthoDB; 2032428at2; -.
DR Proteomes; UP000002166; Chromosome.
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; 2.30.30.170; -; 7.
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; 3.20.20.470; Glucansucrase; 2.
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; IPR025987; GW_dom.
DR InterPro; IPR038200; GW_dom_sf.
DR InterPro; IPR022263; KxYKxGKxW.
DR NCBIfam; TIGR04035; glucan_65_rpt; 2.
DR NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR Pfam; PF01473; Choline_bind_1; 3.
DR Pfam; PF19127; Choline_bind_3; 3.
DR Pfam; PF02324; Glyco_hydro_70; 1.
DR Pfam; PF13457; GW; 7.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR SUPFAM; SSF82057; Prokaryotic SH3-related domain; 7.
DR PROSITE; PS51170; CW; 2.
DR PROSITE; PS51780; GW; 6.
PE 3: Inferred from homology;
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..2057
FT /note="dextransucrase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002768908"
FT REPEAT 175..194
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 1326..1346
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 1491..1582
FT /note="GW"
FT /evidence="ECO:0000259|PROSITE:PS51780"
FT DOMAIN 1584..1663
FT /note="GW"
FT /evidence="ECO:0000259|PROSITE:PS51780"
FT DOMAIN 1664..1742
FT /note="GW"
FT /evidence="ECO:0000259|PROSITE:PS51780"
FT DOMAIN 1743..1821
FT /note="GW"
FT /evidence="ECO:0000259|PROSITE:PS51780"
FT DOMAIN 1899..1979
FT /note="GW"
FT /evidence="ECO:0000259|PROSITE:PS51780"
FT DOMAIN 1980..2057
FT /note="GW"
FT /evidence="ECO:0000259|PROSITE:PS51780"
FT REGION 50..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2057 AA; 228994 MW; 73E557C8B9A3C033 CRC64;
MKQQETVTRK KLYKSGKVWV AAATAFAVLG VSTVTTVNAD TNPNVAVKQI NNTGTNDSGE
KKVPVPSTNN DSLKQGTDGF WYDSDGNRVD QKTNQILLTA EQLKKNNEKN LSVISDDTSK
KDDENISKQT KIANQQTVDT AKGLTTSNLS DPITGGHYEN HNGYFVYIDA SGKQVTGLQN
IDGNLQYFDD NGYQVKGSFR DVNGKHIYFD SVTGKASSNV DIVNGKAQGY DAQGNQLKKS
YVADSSGQTY YFDGNGQPLI GLQTIDGNLQ YFNQQGVQIK GGFQDVNNKR IYFAPNTGNA
VANTEIINGK LQGRDANGNQ VKNAFSTDVA GNTFYFDANG VMLTGLQTIS GKTYYLDEQG
HLRKNYAGTF NNQFMYFDAD TGAGKTAIEY QFDQGLVSQS NENTPHNAAK SYDKSSFENV
DGYLTADTWY RPTDILKNGD TWTASTETDM RPLLMTWWPD KQTQANYLNF MSSKGLGITT
TYTAATSQKT LNDAAFVIQT AIEQQISLKK STEWLRDAID SFVTTQANWN KQTEDEAFDG
LQWLQGGFLA YQDDSHRTPN TDSGNNRKLG RQPVNIDGSK DTTDGKGSEF LLANDIDNSN
PIVQAEQLNW LHYLMNFGSI TGNNDNANFD GIRVDAVDNV DADLLKIAGD YFKALYGTDK
SDANANKHLS ILEDWNGKDP QYVNQQGNAQ LTMDYTVTSQ FGNSLTHGAN NRSNMWYFLD
TGYYLNGDIN KKIVDKNRQN SGTLVNRIAN AGDTQVIPNY SFIRAHDYDA QDPIRRAMID
HGIIKNMQDT FTFDQLAQGM EFYYQDQNNP SGFKKYNDYN LPSAYAMLLT NKDTIPRVYY
GDMYYEGGQY MQNETIYNRI ISALLKARIK YVSGGQTMAT DSSGKDLKDG ETDLLTSVRF
GKGIMTSDQT TTQDNSQDYK NQGIGVIVGN NPDLKLNNDK TITLHMGKAH KNQLYRALAL
SNDSGIDVYN SDDEAPTLRT NDNGDLIFHK TNTFVKQDGT IINYEMKGSL NALISGYLGV
WVPVGASDSQ DARTVATEAS SSNDGSVFHS NAALDSNVIY EGFSNFQAMP TSPEQSTNVV
IAANAEMFKK LGITSFELAP QYRSSGDTNY GGMSFLDSFL NNGYAFTDRY DLGFNKADGT
PNPTKYGTDQ DLRNAIEALH KNGMQAIADW VPDQIYALPG KEVVTATRVD ERGNQLKDTD
FVNLLYVANT KSSGVDYQSK YGGEFLDKLK EEYSSLFKQN QVSTGQPIDA STKIKQWSAK
YMNGTNILHR GAYYVLKDWA TNQYFNVAKT DEVFLPLQLQ NKDSQTGFIS DASGVKYYSI
SGYQAKDTFI EDGNGNWYYF DKDGYMARSQ QGENPIRTVE TSVNTRNGNY YFMPNGVELR
KGFGTDNSGN VYYFDDQGKM VRDKYINDDA NNFYHLNVDG TMSRGLFKFD SDTLQYFASN
GVQIKDSYAK DSKGNKYYFD SATGNNDTVK AQAWDGNGYY ITIDSDANNT IGVNTDYTAY
ITSSLREDGL FANAPYGVVT KDQNGNDLKW QYINHTKQYE GQQVQVTRQY TDSKGVSWNL
ITFAGGDLQG QKLWVDSRAL TMTPFKTMNQ ISFISYANRN DGLFLNAPYQ VKGYQLAGMS
NQYKGQQVII AGVANVSGKD WSLISFNGTQ YWIDSQALNT NFTHDMNQKV FVNTTSNLDG
LFLNAPYRQP GYKLAGLAKN YNNQTVTVSQ QYFDDQGTVW SQVVLGGQTV WVDNHALAQM
QVSDTSQQLY VNSNGRNDGL FLNAPYRGQG SQLIGMTADY NGQHVQVTKQ GQDAYGAQWR
LITLNNQQVW VDSRALSTTI MQAMNDDMYV NSNQRTDGLW LNAPYTMSGA KWAGDTRSAN
GRYVHISKAY SNEVGNTYYL TNLNGQSTWI DKRAFTATFD QVVALNATIV ARQRPDGMFK
TAPYGEAGAQ FVDYVTNYNQ QTVPVTKQHS DAQGNQWYLA TVNGTQYWID QRSFSPVVTK
VVDYQAKIVP RTTRDGVFSG APYGEVNAKL VNMATAYQNQ VVHATGEYTN ASGITWSQFA
LSGQEDKLWI DKRALQA
//
