ID   LSCI_GEOSE              Reviewed;         473 AA.
AC   P94468;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Inactive levansucrase;
DE   Flags: Precursor;
GN   Name=sacB; Synonyms=surB;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae;
OC   Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LACK OF FUNCTION AS A LEVANSUCRASE.
RC   STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB
RC   8923 / NCTC 10339 / R-35646 / VKM B-510;
RX   PubMed=9349714; DOI=10.1016/s0167-4781(97)00103-6;
RA   Li Y., Triccas J.A., Ferenci T.;
RT   "A novel levansucrase-levanase gene cluster in Bacillus stearothermophilus
RT   ATCC12980.";
RL   Biochim. Biophys. Acta 1353:203-208(1997).
RN   [2]
RP   DISCUSSION OF SEQUENCE WITH RESPECT TO INACTIVITY.
RX   PubMed=10377564;
RA   Naumoff D.G.;
RT   "Homologous locus of Bacillus subtilis and Bacillus stearothermophilus
RT   genomes containing levansucrase and levanase genes.";
RL   Mol. Biol. (Mosk.) 33:207-210(1999).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
CC   -!- CAUTION: According to PubMed:9349714, does not have levansucrase
CC       activity, despite a very strong similarity to SacB from B.subtilis.
CC       {ECO:0000305}.
CC   -!- CAUTION: Ser-356 and Gln-363 are present instead of the conserved Phe
CC       and positively charged residue Lys/His/Arg, respectively, which could
CC       be important for activity. These point mutations might explain the
CC       inactivity of the enzyme. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U34874; AAB97111.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94468; -.
DR   SMR; P94468; -.
DR   CAZy; GH68; Glycoside Hydrolase Family 68.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050053; F:levansucrase activity; IEA:InterPro.
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   1: Evidence at protein level;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..473
FT                   /note="Inactive levansucrase"
FT                   /id="PRO_0000012248"
SQ   SEQUENCE   473 AA;  52855 MW;  12F7A272EC2B771E CRC64;
     MNIKKFAKQA TVLTFTTALL AGGATQAFAK ETNQKPYKET YGISHITRHD MLQIPEQQKN
     EKYQVPEFDS STIKNISSAK GLDVWDSWPL QNADGTVANY HGYHIVFALA GDPKNADDTS
     IYMFYQKVGE TSIDSWKTPG RVFKDSDKFD ANDSILKDQT QEWSGSATFT SDGKIRLFYT
     DFSGKHYGKQ TLTTAQVNVS ASDSSLNING VEDYKSIFDG DSKTYQNVQQ FIDEGNYSSG
     DNHTLRDPHY VEDKGHKYLV FEANTGTEDG YQGEESLFNK AYYGKSTSFF RQESQKLLQS
     DKNRTAELAN GALGMIELND DYTLKKVMKP LIASNTVTDE IERANVFKMN GKWYLSTDSR
     GSQMTIDGIT SNDIYMLGYV SNSLTGPYKP LNKTGLVLKM DLDPNDVTFT YSHFAVPQAT
     GNNVVITSYM TNRGFYADKQ STFAPSFLLN IQGKKTSVVK ASILDQGQLT VNQ
//