SACB_BACSU
ID SACB_BACSU Reviewed; 473 AA.
AC P05655; P70984;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 146.
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; OrderedLocusNames=BSU34450;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2993818; DOI=10.1007/bf00425427;
RA Steinmetz M., Le Coq D., Aymerich S., Gonzy-Treboul G., Gay P.;
RT "The DNA sequence of the gene for the secreted Bacillus subtilis enzyme
RT levansucrase and its genetic control sites.";
RL Mol. Gen. Genet. 200:220-228(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
RC STRAIN=168 / PY79;
RX PubMed=6424671; DOI=10.1016/s0006-291x(84)80320-4;
RA Fouet A., Arnaud M., Klier A., Rapoport G.;
RT "Characterization of the precursor form of the exocellular levansucrase
RT from Bacillus subtilis.";
RL Biochem. Biophys. Res. Commun. 119:795-800(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RX PubMed=2428811; DOI=10.1128/jb.168.1.380-388.1986;
RA Shimotsu H., Henner D.J.;
RT "Modulation of Bacillus subtilis levansucrase gene expression by sucrose
RT and regulation of the steady-state mRNA level by sacU and sacQ genes.";
RL J. Bacteriol. 168:380-388(1986).
RN [6]
RP INDUCTION.
RX PubMed=11739774; DOI=10.1099/00221287-147-12-3413;
RA Pereira Y., Petit-Glatron M.-F., Chambert R.;
RT "yveB, encoding endolevanase LevB, is part of the sacB-yveB-yveA
RT levansucrase tricistronic operon in Bacillus subtilis.";
RL Microbiology 147:3413-3419(2001).
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: Induced by sucrose. {ECO:0000269|PubMed:11739774}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR EMBL; M14202; AAA22725.1; -; Genomic_DNA.
DR EMBL; Z94043; CAB08015.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15450.1; -; Genomic_DNA.
DR EMBL; K01987; AAA22724.1; -; Genomic_DNA.
DR EMBL; X02730; CAA26513.1; -; Genomic_DNA.
DR PIR; S07309; A25040.
DR RefSeq; NP_391325.1; NC_000964.3.
DR RefSeq; WP_001022105.1; NZ_JNCM01000033.1.
DR PDB; 1OYG; X-ray; 1.50 A; A=30-473.
DR PDB; 1PT2; X-ray; 2.10 A; A=30-473.
DR PDB; 2VDT; X-ray; 3.20 A; A=34-472.
DR PDB; 3BYJ; X-ray; 2.10 A; A=1-473.
DR PDB; 3BYK; X-ray; 2.10 A; A=1-473.
DR PDB; 3BYL; X-ray; 2.10 A; A=1-473.
DR PDB; 3BYN; X-ray; 2.10 A; A=1-473.
DR PDB; 6PWQ; X-ray; 2.60 A; A/B=30-473.
DR PDB; 6VHQ; X-ray; 2.05 A; A/B=30-473.
DR PDBsum; 1OYG; -.
DR PDBsum; 1PT2; -.
DR PDBsum; 2VDT; -.
DR PDBsum; 3BYJ; -.
DR PDBsum; 3BYK; -.
DR PDBsum; 3BYL; -.
DR PDBsum; 3BYN; -.
DR PDBsum; 6PWQ; -.
DR PDBsum; 6VHQ; -.
DR AlphaFoldDB; P05655; -.
DR SMR; P05655; -.
DR STRING; 224308.BSU34450; -.
DR DrugBank; DB02772; Sucrose.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR PaxDb; P05655; -.
DR PRIDE; P05655; -.
DR EnsemblBacteria; CAB15450; CAB15450; BSU_34450.
DR GeneID; 936413; -.
DR KEGG; bsu:BSU34450; -.
DR PATRIC; fig|224308.179.peg.3732; -.
DR eggNOG; COG1621; Bacteria.
DR InParanoid; P05655; -.
DR OMA; DPWFFED; -.
DR PhylomeDB; P05655; -.
DR BioCyc; BSUB:BSU34450-MON; -.
DR BioCyc; MetaCyc:BSU34450-MON; -.
DR BRENDA; 2.4.1.10; 658.
DR SABIO-RK; P05655; -.
DR EvolutionaryTrace; P05655; -.
DR Proteomes; UP000001570; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..29
FT CHAIN 30..473
FT /note="Levansucrase"
FT /id="PRO_0000012249"
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"
FT CONFLICT 12
FT /note="V -> I (in Ref. 4; AAA22724)"
FT /evidence="ECO:0000305"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:1OYG"
FT TURN 184..188
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 189..201
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 206..218
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6PWQ"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 322..333
FT /evidence="ECO:0007829|PDB:1OYG"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 374..383
FT /evidence="ECO:0007829|PDB:1OYG"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2VDT"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 419..431
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:2VDT"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6VHQ"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:1OYG"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:1OYG"
SQ SEQUENCE 473 AA; 52971 MW; 3FBF2F571B41D5B0 CRC64;
MNIKKFAKQA TVLTFTTALL AGGATQAFAK ETNQKPYKET YGISHITRHD MLQIPEQQKN
EKYQVPEFDS STIKNISSAK GLDVWDSWPL QNADGTVANY HGYHIVFALA GDPKNADDTS
IYMFYQKVGE TSIDSWKNAG RVFKDSDKFD ANDSILKDQT QEWSGSATFT SDGKIRLFYT
DFSGKHYGKQ TLTTAQVNVS ASDSSLNING VEDYKSIFDG DGKTYQNVQQ FIDEGNYSSG
DNHTLRDPHY VEDKGHKYLV FEANTGTEDG YQGEESLFNK AYYGKSTSFF RQESQKLLQS
DKKRTAELAN GALGMIELND DYTLKKVMKP LIASNTVTDE IERANVFKMN GKWYLFTDSR
GSKMTIDGIT SNDIYMLGYV SNSLTGPYKP LNKTGLVLKM DLDPNDVTFT YSHFAVPQAK
GNNVVITSYM TNRGFYADKQ STFAPSFLLN IKGKKTSVVK DSILEQGQLT VNK
