ID   SACB_BACAM              Reviewed;         472 AA.
AC   P21130;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Levansucrase;
DE            EC=2.4.1.10;
DE   AltName: Full=Beta-D-fructofuranosyl transferase;
DE   AltName: Full=Sucrose 6-fructosyl transferase;
DE   Flags: Precursor;
GN   Name=sacB;
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   -!- 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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: By sucrose.
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   BRENDA; 2.4.1.10; 630.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050053; F:levansucrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR   CDD; cd08997; GH68; 1.
DR   Gene3D; 2.115.10.20; -; 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; SSF75005; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Secreted; Signal; Transferase.
FT   SIGNAL          1..29
FT   CHAIN           30..472
FT                   /note="Levansucrase"
FT                   /id="PRO_0000012247"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   ACT_SITE        342
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         246..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         340..342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   SITE            247
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
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