ID   SACB_STRSL              Reviewed;         969 AA.
AC   Q55242;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=ftf;
OS   Streptococcus salivarius.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25975;
RX   PubMed=8331080; DOI=10.1128/jb.175.14.4520-4527.1993;
RA   Rathsam C., Giffard P.M., Jacques N.A.;
RT   "The cell-bound fructosyltransferase of Streptococcus salivarius: the
RT   carboxyl terminus specifies attachment in a Streptococcus gordonii model
RT   system.";
RL   J. Bacteriol. 175:4520-4527(1993).
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, cell wall.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 family. {ECO:0000305}.
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DR   EMBL; L08445; AAA71925.1; -; Genomic_DNA.
DR   RefSeq; WP_045771731.1; NZ_QSAU01000001.1.
DR   AlphaFoldDB; Q55242; -.
DR   SMR; Q55242; -.
DR   CAZy; GH68; Glycoside Hydrolase Family 68.
DR   SABIO-RK; Q55242; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF02435; Glyco_hydro_68; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
PE   3: Inferred from homology;
KW   Cell wall; Glycosyltransferase; Secreted; Signal; Transferase.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..969
FT                   /note="Levansucrase"
FT                   /id="PRO_0000012251"
FT   REGION          89..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..934
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        287
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   ACT_SITE        547
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         448..449
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         545..547
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   BINDING         565
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
FT   SITE            449
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q74K42"
SQ   SEQUENCE   969 AA;  103984 MW;  D389B5B32ACF735A CRC64;
     MDITVNSQSN TVAPKQAECK KMRYSIRKVA TVGATSALVG TLAFLGATQV KADQVTETAP
     AVATATATPE TSTASLTVAS ETATSVATSE AVESSVAHSE VATKPVTETQ PSNTTPSVVE
     EKASSTVVTS SSDATTPSAT VAAVSAPAHT SEAAVEAPTS TASSEAADTH TEVDLKVSEN
     SAANANLSKL NGRIKSIVEE NMTSDQIVAL TEEEIKALNK VDFSDDAIKG TGTSLTYRNL
     KDIVASFLKQ DSKLAVPYFK ADTIINMPAF NTVDAQTMKK EEIDVWDSWP VQDAKSGVVS
     NWNGYQLVIS MAGAPNKNSN HIYLLYRKYG DNDFTHWKNA GPIFGYNALE DDQQWSGSAT
     VNSDGSIQLY YTKNDTSGGK LNWQQLASAT LNLAVENDEV VIKSVENDHI LFGGDNYHYQ
     SYPKFMSTFD DDHNHDGNPD RTDNYCLRDP HIIEDNGSRY LIFESNTGDE NYQGEKQIYK
     WSNYGGDDAF NLKSFLNIVN NKHLYNLASW ANGSIGILKL DDNEKNPSVA ELYTPLVTSH
     MVTDEVERPS VVKMGGKYYL FTASRINKST DAEGTVAARE AVGDDVVMLG FVSDSLRGKY
     RPLNGSGVVL TASVPADWRT STYSYYAVPV EGSSDTLLVT SYMTNRGGIA GAENKSTWAP
     SFLIKMNADD TTEVLPKMTN QGDWIWDKSS ESLVHVGDQN SAKLPNEDFN VDYYAVSGYG
     LKPHTYPTVD GSTGVSEAHG VLTVTVKDGK DKKADKPETP VSPTEGNHSV DDKTNKPGTS
     KPADNNQPSA DKEDKPTNPT NPDSPARTPF PYYGDHSNDN NSSNDHHVAV PVKPSTGDSV
     GDRRPVAQAA EIATPVPKTI VATGPTVPTN TVKEESVTET EAPKPVKSEE KVQSHGVDKA
     NEVTKSDESS KGNNTKVAAK LATTPKTPSD SEGSNSNILS ILATIFAAIA SLALLGYGLV
     TGKIHLPKK