ID A0A0R2JQZ0_9LACO Unreviewed; 1143 AA.
AC A0A0R2JQZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=IV43_GL000457 {ECO:0000313|EMBL:KRN79505.1};
OS Ligilactobacillus acidipiscis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=89059 {ECO:0000313|EMBL:KRN79505.1, ECO:0000313|Proteomes:UP000051491};
RN [1] {ECO:0000313|EMBL:KRN79505.1, ECO:0000313|Proteomes:UP000051491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15353 {ECO:0000313|EMBL:KRN79505.1,
RC ECO:0000313|Proteomes:UP000051491};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN79505.1}.
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DR EMBL; JQBK01000139; KRN79505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2JQZ0; -.
DR SMR; A0A0R2JQZ0; -.
DR STRING; 89059.LAC1533_1991; -.
DR PATRIC; fig|89059.3.peg.466; -.
DR Proteomes; UP000051491; 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; 2.10.270.10; 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; IPR003318; Glyco_hydro70cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF01473; Choline_bind_1; 1.
DR Pfam; PF19127; Choline_bind_3; 2.
DR Pfam; PF02324; Glyco_hydro_70; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
PE 3: Inferred from homology;
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 205..1007
FT /note="Glycoside hydrolase family 70 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02324"
SQ SEQUENCE 1143 AA; 127565 MW; 3A5DDFF8BCDF9768 CRC64;
MTGAMQTGFQ RIPEQAKTVY YDQQGKMSHG QRKINGAWYL FDQNTGAVKV GLQKIADQNK
TVYYDKKTAQ MLKGQQHVDN RWYLFDKVTG AMQTGLRAIP EQKKLVYYDP KNGQMQYGTI
LMDGQNGTKS IFYFDKTTGA LTAIGDQTWY DEAQNDMPFS FDESSMNTVN GYLSWTGWYR
PKGYHQNGQK WVQTGASDWR PYMLYIWPSN DIQAKYIQYF VGHGYTDQSL GLTAKNVNKL
NGSTNSQLLN DYSRKLRDAI EKEIFENNYS TSKLASTMDG FVAFVPEFNG LSELPVEKQP
GYKPDNSGTV DNDQLLFVNS GNGNQKQGNT TNADSQFRNL NHTIWNQYGT EKDGNKFGPE
LLVGNDIDNS NPVVQAENIN WEYFLLKYGE IMGYGSDANF DGFRNDAADN IDADVLDQQA
QLLNDMFDLK GSEANANGHL VYNEGYHSGA ASMLGNKNNQ QLYMDSQEFY TLLNTLGKAN
GKRNKLTDLI TNSVVDRHND NTDSSAQPNW SFVTNHDQRK NVINQIIIDS HPGVTDIMGD
SYKAEYAVQA WEKYYNDELQ TNKQYAIYNV LAQYAILLSN KDTVPQIYYG DMFDETKPYM
ESKSIYYDGI VAMLKARQKY VAGGQSYQSY GDDLIASVRY GKGNASAQAK GSDPLGRTTG
MAVIVSNNPT MQQRTITVAM GKAHANQQYM NLINTTASSS NVGGVSYNSD SILTTDSDGN
LVLTIKGYAN PLVNGYLGVW VPVGAAEDQV ATTADSTAKK SSGKIYESNA ALDSHVIYED
FSLYQPEFAD INKSAYVVLA DHAQDFADMG VTDFWMAPPY TSFSMSRYNE GYSINDRYTL
GTDEAPTKYG TGAQLADALK AIHAAGMKAQ VDMVMNQMIG FPTQEAVTVS RTDNYGNTLS
VDGKTFANEV YLAYTIGGGQ GQSTYGGKFL DELKQKYPDL FTTKAGSTGV APDSSTHITQ
WSAKYENGTS TQNIGIGRVM KEKDGSYDYV ESGNNHLLHT QLPSEFTSEE KWLSNNSQST
GWIHVKGQTY YYDKGTVVLG EQKINGHWYM FDSQTGVMDT GFTNISKAKK TVYYDIDGKM
LYGEQKINGH WYYFDQITGS RATGFKKLSG KTVYYNANGQ MLYGRQVING HVYNFDRVTG
ALK
//
