ID   LSC_BACAM               Reviewed;         472 AA.
AC   P21130;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   04-NOV-2026, entry version 96.
DE   RecName: Full=Levansucrase {ECO:0000303|PubMed:2265762};
DE            Short=LVS {ECO:0000303|PubMed:2265762};
DE            EC=2.4.1.10 {ECO:0000250|UniProtKB:P05655};
DE   AltName: Full=Beta-D-fructofuranosyl transferase;
DE   AltName: Full=Sucrose 6-fructosyl transferase;
DE   Flags: Precursor;
GN   Name=sacB {ECO:0000303|PubMed:2265762};
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 23844 / P;
RX   PubMed=2265762; DOI=10.1016/0378-1119(90)90345-r;
RA   Tang L.B., Lenstra R., Borchert T.V., Vasantha N.;
RT   "Isolation and characterization of levansucrase-encoding gene from Bacillus
RT   amyloliquefaciens.";
RL   Gene 96:89-93(1990).
CC   -!- FUNCTION: Catalyzes the synthesis of levan, a fructose polymer, by
CC       transferring the fructosyl moiety from sucrose to a growing acceptor
CC       molecule (By similarity). Also displays sucrose hydrolase activity (By
CC       similarity). {ECO:0000250|UniProtKB:P05655}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside +
CC         sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-
CC         glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-
CC         COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10;
CC         Evidence={ECO:0000250|UniProtKB:P05655};
CC   -!- ACTIVITY REGULATION: Ca(2+) may play an important structural role and
CC       promote stability of levansucrase. {ECO:0000250|UniProtKB:P05655}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05655}.
CC   -!- INDUCTION: Induced by sucrose when expressed in B.subtilis.
CC       {ECO:0000269|PubMed:2265762}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR   EMBL; X52988; CAA37179.1; -; Genomic_DNA.
DR   PIR; JQ0802; JQ0802.
DR   AlphaFoldDB; P21130; -.
DR   SMR; P21130; -.
DR   STRING; 692420.BAMF_3880; -.
DR   CAZy; GH68; Glycoside Hydrolase Family 68.
DR   eggNOG; COG1621; Bacteria.
DR   OMA; AACMSAH; -.
DR   BRENDA; 2.4.1.10; 630.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0050053; F:levansucrase activity; ISS:UniProtKB.
DR   GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR   CDD; cd08997; GH68; 1.
DR   Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR   InterPro; IPR003469; Glyco_hydro_68.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF02435; Glyco_hydro_68; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Carbohydrate metabolism; Glycosyltransferase; Metal-binding;
KW   Secreted; Signal; Transferase.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..472
FT                   /note="Levansucrase"
FT                   /id="PRO_0000012247"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   ACT_SITE        342
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         85
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         86
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         164
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         241
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         246
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         247
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         272
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         308
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         310
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         339
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         340
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   BINDING         360
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
FT   SITE            247
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P05655"
SQ   SEQUENCE   472 AA;  52859 MW;  F38592D272677E7D CRC64;
     MNIKKIVKQA TVLTFTTALL AGGATQAFAK ENNQKAYKET YGVSHITRHD MLQIPKQQQN
     EKYQVPQFDQ STIKNIESAK GLDVWDSWPL QNADGTVAEY NGYHVVFALA GSPKDADDTS
     IYMFYQKVGD NSIDSWKNAG RVFKDSDKFD ANDPILKDQT QEWSGSATFT SDGKIRLFYT
     DYSGKHYGKQ SLTTAQVNVS KSDDTLKING VEDHKTIFDG DGKTYQNVQQ FIDEGNYTSG
     DNHTLRDPHY VEDKGHKYLV FEANTGTENG YQGEESLFNK AYYGGGTNFF RKESQKLQQS
     AKKRDAELAN GALGIIELNN DYTLKKVMKP LITSNTVTDE IERANVFKMN GKWYLFTDSR
     GSKMTIDGIN SNDIYMLGYV SNSLTGPYKP LNKTGLVLQM GLDPNDVTFT YSHFAVPQAK
     GNNVVITSYM TNRGFFEDKK ATFGPSFLMN IKGNKTSVVK NSILEQGQLT VN
//